Products

Description Bone morphogenetic proteins (BMPs) constitute a subfamily of structurally related signaling proteins within the TGF-β superfamily. Members of this superfamily are widely distributed throughout the body and are involved in various physiological processes both prenatally and postnatally. Like BMP-7, BMP-4 is also involved in the development and maintenance of bone and cartilage. Reduced expression of BMP4 is associated with many skeletal diseases, including the hereditary condition progressive diaphyseal dysplasia. Mature mouse and human BMP-4 have 98% amino acid (aa) homology. This product features high activity, high purity, and low endotoxin levels. It has been validated and tested for bioactivity, endotoxin levels, and SDS-PAGE to ensure the consistency of biological activity and batch-to-batch uniformity. Our product is provided in a carrier-free form, making it highly suitable for research and production of cell culture, ELISA, or immunoblotting standards.   Product Properties Synonyms Bone Morphogenetic Protein 4;BMP4;BMP2B; BMP-2B; BMP2B1; Uniprot No. P21275 Source E.coil-derived Mouse BMP-4 protein,Lys303-Arg408 with His tag at the C-terminus Amino Acid MKKNKNCRRHSLYVDFSDVGWND WIVAPPGYQAFYCHGDCPFPLADHL NSTNHAIVQTLVNSVNSSIPKACCVP TELSAISMLYLDEYDKVVLKNYQEMV VEGCGCR Molecular Weight Approximately 14 kDa. Biological Activity Measure by its ability to induce alkaline phosphatase production by ATDC5 cells. The ED50 for this effect is 10 ng/mL. The specific activity of recombinant mouse BMP-4 is > 1 x 100000 IU/mg. Purity > 98% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1×PBS, pH4.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring  the  contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL.   Shipping and Storage Ice pack shipping. Store at -20°C with a one-year shelf life. Recommended to aliquot and freeze upon first use to avoid repeated freezing and thawing.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.   Usage 1. It is recommended to reconstitute the lyophilized powder with sterile water, ensuring that the solution concentration is not less than 100 μg/mL, and let it stand for at least 20 minutes to fully dissolve. 2. After reconstitution, the solution can be further diluted and aliquoted, stored at 2-8°C with a shelf life of 1 month, and at -20°C with a shelf life of 3 months; avoid repeated freezing and thawing. 3. When further diluting and aliquoting the reconstituted solution, a certain amount of carrier protein should be added (0.1% BSA, 10% FBS, or 5% HSA). For experiments that require serum-free conditions, it can be replaced with a 5% trehalose solution as the carrier.

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Chemokine (C-X-C motif) ligand 14 (CXCL14), also named BRAK, is a small cytokine belonging to the CXC chemokine family. Recombinant mouse CXCL14 contains 77 amino acid residues and it shares 97 % and 99 % a.a. sequence identity with human and rat CXCL14. CXCL14 serves as a chemoattractant for activated macrophages, immature dendritic cells and natural killer cells, as well as an antiangiogenic factor by preventing the migration of endothelial cells. CXCL14 also exerts an inhibitory effect on the CXCL12/ CXCR4 signaling pathway, which is involved in the maintenance of T‐helper (Th)2 bias, and promotes Th1 immune response under the physiological and pathological conditions. CXCL14 has been shown to be a highly selective chemoattractant for monocytes that have been treated with prostaglandin E2 or forskolin, agents that activate adenylate cyclase.   Product Properties Synonyms B-cell and Monocyte-activating Chemokine, Chemokine BRAK, Kidney-expressed Chemokine CXC, CXCL14, MIP-2G, Small-inducible Cytokine B14 Accession Q9WUQ5 GeneID 57266 Source E.coli-derived mouse BRAK/CXCL14 protein, Ser23-Glu99. Molecular Weight Approximately 9.4 kDa. AA Sequence SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIVTTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 1.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 400 mM NaCl, pH 7.4, 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤-20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Cardiotrophin1 (CT1) is a member of the cytokine family which also includes IL-6, IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM), and ciliary neurotrophic factor (CNTF). CT-1 is a pleiotropic cytokine which is expressed in various tissues including the adult heart, skeletal muscle, ovary, colon, prostate and fetal lung. Studies showed CT-1 which induces cardiac myocyte hypertrophy in vitro can bind to and activate the ILST/gp130 receptor. Rat CT1 encodes a 203 amino acid (a.a.) residue protein that lacks a hydrophobic signal peptide and it shares 94% a.a. and 79% a.a. sequence identity with human and murine CT-1.   Product Properties Synonyms CT-1CT1; CTF1 Accession Q60753 GeneID 13019 Source E.coli-derived Mouse CT-1, Met1-Ala203, with an N-terminal Met. Molecular Weight Approximately 21.5 kDa. AA Sequence MSQREGSLED HQTDSSISFL PHLEAKIRQT HNLARLLTKY AEQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSVLPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP GPEPVTVATL FTANSTAGIF SAKVLGFHVC GLYGEWVSRT EGDLGQLVPG GVA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 10 6 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 1 EU/µg of rMuCT-1 as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris, 300 mM NaCl, pH 8.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Ciliary neurotrophic factor (CNTF) is one of a small number of proteins with neurotrophic activities distinct from nerve growth factor (NGF). The cDNA for human CNTF encodes a 200 amino acid residue polypeptide that lacks a signal sequence. Recombinant human CNTF containing 200 amino acids and it shares 82% and 83% a.a. sequence identity with mouse and rat CNTF. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. CNTF is structurally related to IL-6, IL-11, LIF and OSM. Among factors belonging to the CNTF family, CNTF, leukemia inhibitory factor, cardiotrophin-1, and oncostatin M induced a strong promyelinating effect.   Product Properties Synonyms ciliary neurotrophic factor, CNTF, HCNTF Accession P51642 GeneID 12803 Source E.coli-derived mouse CNTF, Ala2-Met198. Molecular Weight Approximately 22.5 kDa. AA Sequence AFAEQSPLTL HRRDLCSRSI WLARKIRSDL TALMESYVKH QGLNKNISLD SVDGVPVAST DRWSEMTEAE RLQENLQAYR TFQGMLTKLL EDQRVHFTPT EGDFHQAIHT LTLQVSAFAY QLEELMALLE QKVPEKEADG MPVTIGDGGL FEKKLWGLKV LQELSQWTVR SIHDLRVISS HHMGISAHES HYGAKQM Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 30 ng/mL, corresponding to a specific activity of > 3.3 × 10 4 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in in 2 × PBS, pH 7.4, 2% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CTACK is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant Murine CTACK is a 10.9 kDa protein containing 95 amino acid residues.   Product Properties Synonyms CCL27 Accession Q9Z1X0 GeneID 20301 Source E.coli-derived Mouse CCL27 protein,Leu26-Asn120. Molecular Weight Approximately 10.9 kDa AA Sequence LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml. Endotoxin <1 EU/μg of protein as determined by LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 2 × PBS, pH 7.4, with 5% trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL16 is a member of the CXC chemokine family. Mouse CXCL16 has 246 a.a. and consists of a 26 a.a. residue putative signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucin-like spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail. Mouse and human CXCL16 share 49% overall aa identity and 70% similarity in the chemokine domains. CXCL16 is a transmembrane chemokine and is implicated in activated CD8+ T cell trafficking. CXCL16 mediates adhesion and phagocytosis of both Gram-negative and Gram-positive bacteria and is a strong chemoattractant for CXCR6+ T cells. It facilitates uptake of low density lipoproteins by macrophages, resulting in foam cell formation.   Product Properties Synonyms SR-PXOX, Scavenger Peceptor for Phosphatidylserine and Oxidized Low Density Lipoprotein, Small-inducible Cytokine B16, Transmembrane Chemokine CXCL16 Accession Q8BSU2 GeneID 66102 Source E.coli-derived mouse CXCL16 protein, Asn27-Pro114. Molecular Weight Approximately 9.9 kDa. AA Sequence NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using mouse lymphocytes is in a concentration of 20-1000 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CXCL3, also known as DCIP1 in mouse, CINC2 in rat, and GROγ in humans, is belonging to the CXC chemokine family. The amino acid sequence of mouse CXCL3 is 57 % identical to human CXCL3. CXCL3 plays a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils. CXCL3 was reportedly associated with the invasion and metastasis of various malignancies. As a member of the chemokine family, CXCL3 was previously known to participate in many pathophysiological events. CXCL3 was found to be upregulated in aggressive cancer cells.   Product Properties Synonyms chemokine (C-X-C motif) ligand 3, CINC-2, CINC-2b, CXCL3, Dcip1, Gm1960, GRO gamma, GRO3 oncogene, GRO3, GROG, GRO-gamma, Growth-regulated protein gamma, Macrophage inflammatory protein 2-beta, MGSA gamma, MIP2B, MIP-2b, MIP2-beta, SCYB3 Accession Q6W5C0 GeneID 330122 Source E.coli-derived mouse DCIP-1/CXCL3 protein, Ala28-Ser100. Molecular Weight Approximately 7.9 kDa. AA Sequence AVVASELRCQ CLNTLPRVDF ETIQSLTVTP PGPHCTQTEV IATLKDGQEV CLNPQGPRLQ IIIKKILKSG KSS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected human 293 cells is in a concentration range of 10-100 ng/ml. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Desert Hedgehog (Dhh) belongs to the highly conserved Hedgehog family of proteins which are involved in multiple developmental processes. Hedgehogs are synthesized as 45 kDa precursors that are cleaved autocatalytically. The 19 kDa N-terminal fragment remains membrane associated due to its cholesterol and palmitate modifications. Binding of this fragment to Patched receptors results in the loss of Patched repression of Smoothened signaling. Dhh binds both Patched and Patched 2 as well as Hedgehog interacting protein (Hip)\. Within the N-terminal peptide, mouse Dhh shares 97% and 100% amino acid (aa) sequence identity with human and rat Dhh, respectively. It shares 74% aa seqeuence identity with mouse Indian (Ihh) and Sonic hedgehog (Shh). Dhh is produced by Sertoli cells and is required for testis development and spermatogenesis. It induces steroidogenic factor 1 which is instrumental in promoting Leydig cell differentiation. It also promotes the deposition of basal lamina surrounding seminiferous tubules. In humans, mutations of Dhh are associated with pure gonadal dysgenesis. Dhh is expressed in the female by ovarian granulosa cells and the corpus luteum. Its upregulation in human ovarian cancer correlates positively with proliferative index and negatively with prognosis. Dhh is also expressed by Schwann cells and is upregulated following nerve injury. It induces the expression of Patched and Hip in nerve fibroblasts and promotes the formation of the connective tissue sheath surrounding peripheral nerves.   Product Properties Synonyms DHH; HHG-3MGC35145 Accession Q61488 GeneID 13363 Source E.coli-derived Mouse DHH C23II, Cys23-Gly198 Molecular Weight Approximately 20.0 kDa. AA Sequence IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASGPAEGRVTRGSERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDEDGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 μg/ml. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 1 mM DTT, 0.05% Tween-80. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Epidermal growth factor (EGF) is a small, potent growth factor capable of inducing cell proliferation, differentiation, and survival. EGF is the founding member of the EGF family that also includes TGF-alpha, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin- binding EGF-like growth factor (HB-EGF), epigen, and the neuregulins (NRG)-1 through -6. Members of The EGF family are characterized by a shared structural motif, the EGF-like domain, which contains three intramolecular disulfide bonds that are formed by six similarly spaced, conserved cysteine residues. These disulfide bonds are essential for proper protein conformation and receptor binding. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The full length EGF protein is 1207 amino acids (aa) (EGF precursor) containing nine EGF domains and nine LDLR class B repeats. However, the mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region. EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. Physiologically, EGF is found in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. EGF is a high affinity ligand of the EGF receptor (ErbB). Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members. EGF binding induces dimerization of the EGF receptor resulting in activation of the protein tyrosine kinase signaling pathway. These receptors undergo a complex pattern of ligand-induced homo- or hetero-dimerization to transduce EGF family signals. EGF binds ErbB1 and depending on the context, induces the formation of homodimers or heterodimers containing ErbB2.     Product Properties Synonyms Urogastrone, URG Accession P01132 GeneID 13645 Source E.coli-derived Mouse EGF, Asn977-Arg1029. Molecular Weight Approximately 6.0 kDa. AA Sequence NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/mL, corresponding to a specific activity of > 1.0×107 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Endocrine gland-derived vascular endothelial growth factor (EG-VEGF), also called prokineticin 1 (PK1), is a member of the prokineticin family of secreted proteins that share a common structural motif containing ten conserved cysteine residues that form five pairs of disulfide bonds. The mature region in mouse is 93% and 87% aa identical to the mature regions in rat and human. Mouse EG- VEGF stimulates proliferation and survival of liver sinusoidal endothelial cells, and, in mouse, EG-VEGF acts to induce monocyte migration and stimulate hematopoiesis.   Product Properties Synonyms EGVEGF, Mambakine, PROK1, Prokineticin 1 Accession Q14A28 GeneID 246691 Source E.coli-derived Mouse EG-VEGF protein, Ala20-Phe105. Molecular Weight Approximately 9.6 kDa. AA Sequence AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as Measured in a cell proliferation assay using EJG bovine adrenal-derived endothelial cells. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH7.4, with 3% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Product Properties Synonyms   EPO; Erythropoietin; EP; MVCD2; Epoetin   Source HEK293 Cells Molecular Weight The recombinant mouse Epo predicts a molecular mass of 18.6 kDa. AA Sequence NP_031968.1 ((Met1-Arg192) Biological Activity Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is typically 2-10 ng/mL. Purity > 95% by SDS-PAGE. Endotoxin <1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2. This product is for research use only.

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Fatty acid binding proteins (FABP) are small cytoplasmic lipid binding proteins that are expressed in a tissue specific manner and are involved in intracellular lipid transport. All FABPs bind free fatty acids, cholesterol, and retinoids, which differ in their selectivity, affinity and binding mechanism (1). Circulating FABP levels are used as indicators of tissue damage. Some FABP polymorphisms have been associated with disorders of lipid metabolism and the development of atherosclerosis (2). FABPs are structurally conserved, consisting of a water-filled, ligand-binding pocket surrounded by ten anti-parallel beta-barrel structures, capped by an N-terminal helix-turn-helix motif. The helical N-terminus is involved in the regulation of FA transfer from membranes (3).FABP1, also known as liver FABP (L-FABP) is highly expressed in the liver, intestine, kidney and lung (1). FABP1 binds free fatty acids and their co-enzyme A derivatives. FABP1 is unique among other members in FABP family, attributed to its ability to bind multiple ligands at once. It has a larger solvent-accessible core in comparison to other FABPs, and this allows for more diverse binding to substrates (1). Mouse FABP1 is 127 amino acids (aa) in length. It is a two beta-sheet molecule that contains an acetylated initiating methionine. Full-length mouse FABP1 shares 94% and 84% aa identity with rat and human FABP1, respectively (4).   Product Properties Synonyms FABP1; FABPL; fatty acid binding protein 1, liver; fatty acid-binding protein, liver; LFABP; L-FABP; L-FABPFatty acid-binding protein 1; Liver-type fatty acid-binding protein Accession P12710 GeneID 14080 Source E.coli-derived Mouse FABP1, with an N-terminal Met Molecular Weight Approximately 14.2 kDa. AA Sequence MNFSGKYQLQ SQENFEPFMK AIGLPEDLIQ KGKDIKGVSE IVHEGKKIKL TITYGPKVVR NEFTLGEECE LETMTGEKVK AVVKLEGDNK MVTTFKGIKS VTELNGDTIT NTMTLGDIVY KRVSKRI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The binding affinity of rMuFABP1 for the synthetic ligand cis-parinaric acid has been measured by fluorescence titration. Half maximal fluorescence of 2.5 μM rMuFABP1 is achieved with approximately 5 μM cis-paranaric acid. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 2 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fgf-8 is a member of the fibroblast growth factor (FGF) family that was initially identified as an androgen-inducible growth factor in a mammary carcinoma cell line. Fgf-8 is one of the key signaling molecules implicated in the initiation, outgrowth, and patterning of vertebrate limbs. The cloned 1.26-kb cDNA contained an open reading frame encoding 212 amino acid residues with 84%, 86%, and 80% amino acid identities to those of Xenopus, chick, and mouse, respectively. None of the FGF-8 isoforms exhibited activity to FGFR1b, 2b, 3b, but FGFR2c, 3c and FGFR4 can be activated by several FGF-8 isoforms. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration, and it is required for normal brain, eye, ear and limb development during embryogenesis. FGF-8 shows limited expression in the normal adult, but low levels are found in the reproductive and genitourinary tract, peripheral leukocytes and bone marrow hematopoietic cells.    Product Properties Synonyms AIGF, AIGFKAL6, HBGF-8, FGF-8c Accession P37237 GeneID 14179 Source E.coli-derived mouse FGF-8, Gln23-Arg268. Molecular Weight Approximately 28.1 kDa. AA Sequence QVRSAAQKRG PGAGNPADTL GQGHEDRPFG QRSRAGKNFT NPAPNYPEEG SKEQRDSVLP KVTQRHVREQ SLVTDQLSRR LIRTYQLYSR TSGKHVQVLA NKRINAMAED GDPFAKLIVE TDTFGSRVRV RGAETGLYIC MNKKGKLIAK SNGKGKDCVF TEIVLENNYT ALQNAKYEGW YMAFTRKGRP RKGSKTRQHQ REVHFMKRLP RGHHTTEQSL RFEFLNYPPF TRSLRGSQRT WAPEPR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 5.0 ng/mL, corresponding to a specific activity of >2.0×105 IU/mg in the presence of 10 μg/ml of heparin. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 500 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor 16 (FGF-16) belongs to the large FGF family. All FGF family members are heparin-binding growth factors with a core 120 amino acid (a.a.) FGF domain that allows for a common tertiary structure. FGF-16 was originally identified in rat heart tissue by homology based polymerase chain reaction. Murine FGF-16 cDNA predicts a 207 aa precursor protein with one N-linked glycosylation site. FGF-16 lacks a typical signal peptide, but is efficiently generated by mechanisms other than the classical protein secretion pathway. Among FGF family members, FGF-16 is most similar to FGF-9, sharing 73% aa sequence homology. Murine FGF-16 shares 99.5% and 99% aa sequence identity with the human and rat FGF-16, respectively   Product Properties Synonyms Fibroblast growth factor 16；FGF-16 Accession Q9ESL8 GeneID 80903 Source E.coli-derived mouse FGF 16 protein, Met1-Arg207 Molecular Weight Approximately 23.8 kDa. AA Sequence MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Data not available. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Supplied as a 0.2 μm filtered solution in 20 mM Tris-HCl, pH 9.0, 1 M NaCl, 0.02 % Tween-20, 10 % Glycerol. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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FGF-17 is a member of the FGF superfamily of heparin-binding mitogenic molecules characterized by the presence of a core, 120 amino acid (aa) beta-trefoil structure. The mRNA of FGF-17 was found in midgestation of embryo and multiple adult tissues, and is preferentially expressed in specific sites, such as embryonic brain, developing skeleton and arteries.   Product Properties Synonyms FGF-13 Protein; FGF-17 Protein; HH20 Protein Accession P63075 GeneID 1417 Source E.coli-derived mouse FGF 17 protein, Thr23-Thr216 Molecular Weight Approximately 22.5 kDa. AA Sequence TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0×105 IU/mg in the presence of 10 μg/ml of heparin. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 700 mM NaCl, with 0.02 % Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast Growth Factor 18 (FGF-18) is a 20 kDa protein that plays an important role in skeletal development and bone homeostasis. Mature mouse FGF-18 shares 99% amino acid sequence identity with human and rat FGF-18. It is expressed in embryonic somites and the neural fold, adult lung, cerebellar and hippocampal neurons, hair follicle root sheath cells, and osteogenic mesenchymal cells. FGF-18 binds to FGF R2c, FGF R3c as well as the Golgi protein GLG1 and induces the proliferation of astrocytes and microglia, vascular endothelial cells, dermal fibroblasts, papilla cells, and keratinocytes. FGF-18 is required for normal skeletal development. It recruits osteoclasts and osteoblasts to the growth plate, promotes osteoclast formation and function, inhibits osteoblast differentiation, promotes skeletal vascularization, and induces chondrocyte hypertrophy and cartilage matrix formation.   Product Properties Synonyms zFGF5 Accession O89101 GeneID 14172 Source E.coli-derived Mouse FGF-18, Glu28-Gly207. Molecular Weight Approximately 21.0 kDa. AA Sequence EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQAELQK PFKYTTVTKR SRRIRPTHPG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0×106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 500 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor-9, also called FGF-9, is an approximately 26 kDa secreted glycoprotein of the FGF family. Secreted human FGF-9 is a 205-207 aa protein that lacks the N-terminal 1-3 aa and shares 98% sequence identity with mouse, rat, equine, porcine and bovine FGF-9. In addition to FGF R3 (IIIb), FGF-9 binding to the IIIc splice forms of FGF R1, R2 and R3 are variably reported. FGF-9 is an autocrine/paracrine growth factor considered to be important for the growth and survival of motorneurons and prostate. Meanwhile, FGF9 is a potent mitogen and survival factor required for morphogenesis during embryonic development and numerous biological functions at adulthood. FGF9 have been shown to improve systolic function after myocardial infarction in a clinical trial. FGF9 promotes cardiac vascularization during embryonic development but is only weakly expressed in the adult heart.   Product Properties Synonyms FGF9, FGF-9, Glia-activating factor, GAF, glia-activating factor, HBFG-9, HBGF-9 Accession P54130 GeneID 14180 Source E.coli-derived mouse FGF-9, Pro3-Ser208, with an N-terminal Met. Molecular Weight Approximately 23.4 kDa. AA Sequence MPLGEVGSYF GVQDAVPFGN VPVLPVDSPV LLNDHLGQSE AGGLPRGPAV TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY KDILSQS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than0.5 ng/mL, corresponding to a specific activity of > 2.0×106 IU/mg. Fully biologically active whencompared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 500 mM NaCl, pH 8.5. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q.     Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession O3518 GeneID 20312 Source E.coli-derived mouse  Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.7 kDa. AA Sequence QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 μg/mL, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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The glia maturation factor beta belongs to the actin-binding proteins ADF family, GMF subfamily. It contains an ADF-H domain, but the research of crystallography and NMR reveals that there are structures different between human and mouse ADF-H domain. GMF-β is involved in the differentiation, maintenance, and regeneration of the nervous system. It also inhibition of proliferation of tumor cells.   Product Properties Synonyms Glia maturation factor beta, GMF-beta, GMFB Accession Q9CQI3 GeneID 63985 Source E.coli-derived mouse Glia Maturation Factor beta protein, Ser-His142 Molecular Weight Approximately 16.6 kDa. AA Sequence SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity Data not available.   Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-β superfamily. It is a founding member of the GDNF family of ligands (GFL) and has been shown to interact with GFRA2 and GDNF family receptor alpha. Mature rat and human GDNF exhibit approximately 93% amino acid sequence identity and show considerable species cross-reactivity. Cells known to express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells, neurons, pinealocytes and skeletal muscle cells. In embryonic midbrain cultures, recombinant human GDNF promoted the survival and morphological differentiation of dopaminergic neurons and increased their high-affinity dopamine uptake.   Product Properties Synonyms Astrocyte-derived trophic factor, ATF, ATF-1, ATF2, GDNF, HFB1-GDNF, HGDNF, HSCR3 Accession P48540 GeneID 14573 Source E.coli-derived mouse GDNF, Ser78-Ile211. Molecular Weight Approximately 29.9 kDa. AA Sequence SPDKQAAALP RRERNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 0.2 ng/mL, corresponding to a specific activity of > 5.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 0.05% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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GM-CSF is a powerful growth and differentiation factor which acts on hematopoietic progenitor cells and also activates differentiated granulocytes and macrophages.   Product Properties   Synonyms Granulocyte-Macrophage Colony-Stimulating Factor, GM-CSF, CSF-2, MGI-1GM, Pluripoietin-α Source Recombinant Mouse GM-CSF Protein is expressed from Yeast with N-HIS. It contains Ala18-Lys141. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4,with 1%BSA. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 2-7 days, 2~8 °C under sterile conditions after reconstitution.&nbsp; 3 months,&nbsp; -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used&nbsp;and avoid repeated freeze-thaw cycles. Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q.   Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession cytokine D1 GeneID 20312 Source E.coli-derived Mouse Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.7 kDa. AA Sequence QHLGMTKCEI MCGKMTSRIP VALLIRYQLN QESCGKRAIV LETTQHRRFC ADPKEKWVQD AMKHLDHQAA ALTKNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human peripheral blood lymphocytes (PBL) is less than 0.5 μg/mL, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Growth Differentiation Factor-5 (GDF-5; also called BMP-14 and CDMP-1) is a member of the BMP family of TGF-beta superfamily proteins. Mature mouse GDF-5 shares 99% aa sequence identity with both mature human and rat GDF-5. Growth/differentiation factors (GDF-1 to GDF-15) are members of the BMP family of TGF-beta superfamily proteins. They are produced as inactive preproproteins which are then cleaved and assembled into active secreted homodimers. GDF dimers are disulfide-linked with the exception of GDF-3 and -9. GDF proteins are important during embryonic development, particularly in the skeletal, nervous, and muscular systems. GDF-5 is involved in multiple developmental processes including limb generation, cartilage development, joint formation, bone morphogenesis, cell survival, and neuritogenesis.   Product Properties Synonyms CDMP-1, GDF5, OS5, radotermin, SYNS2 Accession P43027 GeneID 14563 Source E.coli-derived mouse GDF-5/BMP-14 protein, Ala376-Arg495. Molecular Weight Approximately 27.2 kDa. AA Sequence APLANRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of mouse ATDC5 cells is less than 1.0 μg/ml, corresponding to a specific activity of > 1000 IU/mg. Fully biologically active when compared to standard.  Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Growth/differentiation factors (GDF-1 to GDF-15) are members of the BMP family of TGF-beta superfamily proteins. At the amino acid level, mature human GDF-7 shares 85% and 88% aa sequence identity with mature GDF-7 in mouse and rat. They are produced as inactive preproproteins which are then cleaved and assembled into active secreted homodimers. GDF dimers are disulfide-linked with the exception of GDF-3 and -9. GDF proteins are important during embryonic development, particularly in the skeletal, nervous, and muscular systems. GDF-7 is involved in tendon and ligament formation and repair. GDF-7 also regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance in the central nervous system.   Product Properties Synonyms BMP12, GDF7, growth differentiation factor 7 Accession P43029 GeneID 238057 Source E.coli-derived mouse GDF-7/BMP-12 protein, Thr316-Arg461. Molecular Weight Approximately 29.8 kDa. AA Sequence TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of mouse ATDC5 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2000 IU/mg. Fully biologically active when compared to standard.  Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Heparin-binding epidermal growth factor (HB-EGF)-like growth factor (EGF) is found in cerebral neurons. Human HB-EGF- shares 76% and 73% aa sequence identity with rat and mouse HB-EGF. Its expression is increased after hypoxic or ischemic injury, which also stimulates neurogenesis. HB-EGF has been implicated as a participant in a variety of normal physiological processes such as blastocyst implantation and wound healing, and in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. The protein is an 86 amino acid mitogenic and chemotactic glycoprotein containing an EGF-like domain with six conserved cysteine residues.   Product Properties Synonyms HBEGF, DT-R Accession Q06186 GeneID 15200 Source E.coli-derived mouse HB-EGF protein, Asp63-Leu148. Molecular Weight Approximately 9.8 kDa. AA Sequence DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using mouse Balb/c 3T3 cells is less than 1 ng/mL, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM PBS, 500 mM NaCl, pH7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interferon-gamma (IFN-γ), also known as Type II interferon or immune interferon, is a pleiotropic cytokine which is now recognised as an important modulator of the immune response. Mature human IFN-γ exists as a non-covalently linked homodimer of 20-25 kDa variably glycosylated subunits.    Product Properties Synonyms Interferon-gamma, IFN-γ, IFG, IFI, IFNG, IFNgamma, IFN-gamma. Accession P01580 GeneID 15978 Source E.coli-derived mouse IFN-γ protein, His23-Cys155. Molecular Weight Approximately 15.5 kDa. AA Sequence HGTVIESLES LNNYFNSSGI DVEEKSLFLD IWRNWQKDGD MKILQSQIIS FYLRLFEVLK DNQAISNNIS VIESHLITTF FSNSKAKKDA FMSIAKFEVN NPQVQRQAFN ELIRVVHQLL PESSLRKRKR SRC Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE  analyses. Biological Activity The ED50 as determined by an anti-viral assay using murine L929 cells infected with encephalomyocarditis (EMC) virus is less than 0.8 ng/ml, corresponding to a specific activity of > 1.3×106 IU/mg. Fully biologically active when compared tostandard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-1 beta (IL-1β) is a pro inflammatory cytokine, which is secreted by immune cells to trigger inflammation and this has been found profoundly in the lesions caused by Leishmania pathogens. IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL-1F1) and IL-1 beta (IL-1F2), which are the products of distinct genes. IL-1 alpha and IL-1 beta are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both IL-1α and IL-1β binds to the same receptor and has similar but not identical biological properties; The mature human IL1β shares 96% amino acid sequence identity with rhesus and 67% -78% with canine, mouse and rat IL-1β.IL-1β, are known to modulate effects of neurotoxic neurotransmitters discharged during excitation or inflammation in the central nervous system (CNS).   Product Properties Synonyms Interleukin-1 beta, IL-1β, IL-1, IL1B, IL-1b, IL1-BETA, IL-1F2, IL1F2IL-1 beta, interleukin-1 beta, preinterleukin 1 beta, pro-interleukin-1-beta. Accession P10749 GeneID 16176 Source E.coli-derived human IL-1β protein, Vla118-Ser269. Molecular Weight Approximately 17.5 kDa. AA Sequence VPIRQLHYRL RDEQQKSLVL SDPYELKALH LNGQNINQQV IFSMSFVQGE PSNDKIPVAL GLKGKNLYLS CVMKDGTPTL QLESVDPKQY PKKKMEKRFV FNKIEVKSKV EFESAEFPNW YISTSQAEHK PVFLGNNSGQ DIIDFTMESV SS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 2 pg/mL, corresponding to a specific activity of > 5.0 × 108 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4, with 5% trehalose, 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-10 (IL-10), also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL-10 family of α-helical cytokines that also includes IL-19, IL-20, IL-22, IL-24, and IL-26/AK155. IL-10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer. Mature human IL- 10 shares 72%- 86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL- 10. IL-10, a cytokine produced by CD4+ T lymphocytes belonging to the Th-2 subset, has previously been shown to inhibit the synthesis of IFN-gamma by both T cells and NK cells.The anti-inflammatory actions of IL-10 may be therapeutically useful either directly or through modulation of HO-1 activity.   Product Properties Synonyms Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, IL10A, TGIF, CSIF Accession P18893 GeneID 16153 Source E.coli-derived mouse IL-10 protein, Ser19-Ser178. Molecular Weight Approximately 18.7 kDa. AA Sequence SRGQYSREDN NCTHFPVGQS HMLLELRTAF SQVKTFFQTK DQLDNILLTD SLMQDFKGYL GCQALSEMIQ FYLVEVMPQA EKHGPEIKEH LNSLGEKLKT LRMRLRRCHR FLPCENKSKA VEQVKSDFNK LQDQGVYKAM NEFDIFINCI EAYMMIKMKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine MC/9-2 cells is less than 1 ng/mL, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10 mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL-11 is a pleiotropic cytokine in the IL-6 family, which also includes LIF, CNTF, Oncostatin M, Cardiotrophin-1, IL-27 and IL-31. IL11 is also known under the names adipogenesis inhibitory factor (AGIF) and oprelvekin.The mouse IL-11 cDNA encodes a 199 amino acid (aa) precursor, which generates a 178 aa, 19 kDa mature unglycosylated protein. It is found in the plasma mainly during inflammation, and is considered to be primarily anti- inflammatory. It stimulates hematopoiesis and thrombopoiesis, regulates macrophage differentiation, and confers mucosal protection in the intestine. It has also been found to enhance T cell polarization toward Th2, promote B cell IgG production, increase osteoclast bone absorption, protect endothelial cells from oxidative stress, and regulate epithelial proliferation and apoptosis. IL-11 synergizes with several other cytokines to produce these effects, and its effects overlap with those of IL-6. IL-11 stimulates the growth of certain lymphocytes and, in the murine model, stimulates an increase in the cortical thickness and strength of long bones. As a signaling molecule, IL-11 has a variety of functions associated with its receptor interleukin 11 receptor alpha; such functions include placentation and to some extent of decidualization.   Product Properties Synonyms AGIF Accession P47873 GeneID 16156 Source E.coli-derived Mouse IL-11, Pro22-Leut199, with an N-terminal Met. Molecular Weight Approximately 19.1 kDa. AA Sequence MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine T11 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-13 (IL-13) was first recognized for its effects on B cells and monocytes, where it upregulated class II expression, promoted IgE class switching and inhibited inflammatory cytokine production. IL-13 is a monomeric 17 kDa immunoregulatory cytokine that plays a key role in the pathogenesis of allergy, cancer, and tissue fibrosis. Mature human IL-13 shares approximately 58% amino acid sequence identity with mouse and rat IL-13. It has become evident that IL-13 is a key mediator in the pathogenesis of allergic inflammation, and IL-13 is key proinflammatory cytokines in asthma. The cytokines interleukin IL-13 have pleiotropic effects on a variety of cell types and impact both pathologic changes and tissue remodeling.   Product Properties Synonyms BHR1interleukin-13, IL13, interleukin 13, MGC116786, NC30, P600 Accession P20109 GeneID 16163 Source E.coli-derived Mouse IL-13, Pro22-Phe131, with an N-terminal Met. Molecular Weight Approximately 12.3 kDa. AA Sequence MPVPRSVSLP LTLKELIEEL SNITQDQTPL CNGSMVWSVD LAAGGFCVAL DSLTNISNCN AIYRTQRILH GLCNRKAPTT VSSLPDTKIE VAHFITKLLS YTKQLFRHGP F Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 4 ng/mL, corresponding to a specific activity of > 2.5 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-18 (IL-18) is a potent pro-inflammatory cytokine that can induce the production of interferon-gamma in Th1 cells, NK cells, and activated macrophages, especially in the presence of IL-12. IL-18 also plays a role in developmental regulation. This product features high activity, high purity, and low endotoxin levels. The product is verified and tested for biological activity, endotoxin levels, and through SDS-PAGE to ensure the biological activity and batch-to-batch consistency; our product is provided in a carrier-free form, making it highly suitable for research and production in cell culture, ELISA, or as a standard for immunoblotting. Product Properties Aliases Interleukin 18; Interleukin-18 Uniprot No. P70380 Expression Range and System E.coli-derived Mouse IL-18 protein, Asn36-Ser192 with a His tag at the C-terminus. Molecular Weight Approximately 18 kDa. Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity Greater than 98% as determined by SDS-PAGE. Activity Measured by its ability to induce IFN gamma secretion in KG-1 cells. The ED50 for this effect is 0.5 μg/mL. Endotoxin Less than 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized (freeze-dried) from a solution containing 1×PBS, pH 8.0.   Usage Instructions 1.It is recommended to reconstitute the lyophilized powder with sterile water to a concentration of no less than 100 μg/mL and let it stand for at least 20 minutes to ensure complete dissolution. 2.After reconstitution, the solution can be further diluted and aliquoted for storage at 2-8°C with a shelf life of 1 month, or at -20°C with a shelf life of 3 months; avoid repeated freeze-thaw cycles. 3.When further diluting and aliquoting the reconstituted solution, it is necessary to add a certain amount of carrier protein (0.1% BSA, 10% FBS, or 5% HSA). For serum-free experimental requirements, it can be replaced with a 5% trehalose solution as the carrier.   Shipping and Storage Ice Pack Shipping:Store at -20°C, with a one-year shelf life. Recommendation for Initial Use: It is advised to aliquot and freeze the product for storage upon the first use to prevent repeated freezing and thawing.   Cautions 1. For your safety and health, please wear a lab coat and use disposable gloves when handling. 2.This product is for research use only.

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Interleukin-2(IL-2) is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. It is expressed by CD4+ and CD8+ T cells, γδ T cells, B cells, dendritic cells, and eosinophils. IL-2/IL-2R signaling is required for T- cell proliferation and other fundamental functions which are essential for the immune response. The receptor for IL-2 consists of three subunits (55 kDa IL-2Rα, 75 kDa IL-2Rβ, and 64 kDa common gamma chain γc/IL-2Rγ) that are present on the cell surface in varying preformed complexes. Mature human IL-2 shares 56% and 66% amino acid sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit cross-species activity.   Product Properties Synonyms Interleukin-2,IL-2,T-cell Growth Factor, TCGF, Aldesleukin Accession P04351 GeneID 16183 Source E.coli-derived mouse IL-2 protein, Ala21-Gln169 Molecular Weight Approximately 17.2 kDa. AA Sequence APTSSSTSSS TAEAQQQQQQ QQQQQQHLEQ LLMDLQELLS RMENYRNLKL PRMLTFKFYL PKQATELKDL QCLEDELGPL RHVLDLTQSK SFQLEDAENF ISNIRVTVVK LKGSDNTFEC QFDDESATVV DFLRRWIAFC QSIISTSPQ Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 0.2 ng/mL, corresponding to a specific activity of > 5.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL-23 is a proinflammatory, heterodimeric protein composed of two subunits: a unique p19 subunit, and a p40 subunit that is shared with IL-12. IL-23 is secreted by activated dendritic cells and macrophages, and signals though a receptor comprised of IL-23R complexed with IL-12Rβ1. IL-23 has been shown to enhance proliferation of memory T cells.   Product Properties   Synonyms Interleukin-23 Source HEK293 Cells Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from sterile PBS, pH7.4. Normally 5% - 8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation. At the amino acid sequence level, mature human and mouse IL-3 share only 29% sequence identity. Consistent with this lack of homology, IL-3 activity is highly species-specific and human IL-3 does not show activity on murine cells. Cytokines are actively involved in the host-defense system to coordinate the functional activity and the generation of effector cells. Some of these molecules function as inflammatory mediators and hematopoietic growth factors at the same time such as IL-3. IL-3 is known as a pleiotropic cytokine with a broad spectrum of target cells and functions. IL-3 regulates the proliferation and differentiation of normal hematopoietic progenitor cells in the early stages of hematopoiesis. And IL-3 inhibits apoptosis and promotes the autonomous growth of blast cells.   Product Properties Synonyms Interleukin-3, IL-3, Hematopoietic growth factor, MCGF, Multipotential colony-stimulating factor, P-cell-stimulating factor Accession P01586 GeneID 16187 Source E.coli-derived mouse IL-1alpha protein, Asp33-Cys166. Molecular Weight Approximately 14.8 kDa. AA Sequence DTHRLTRTLN CSSIVKEIIG KLPEPELKTD DEGPSLRNKS FRRVNLSKFV ESQGEVDPED RYVIKSNLQK LNCCLPTSAN DSALPGVFIR DLDDFRKKLR FYMVHLNDLE TVLTSRPPQP ASGSVSPNRG TVEC Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by the dose-dependent stimulation of the proliferation of murine M-NFS-60 cells is less than 0.05 ng/mL, corresponding to a specific activity of > 2 × 107  IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Insulin-like Growth Factor I (IGF-I), is the dominant effector of Growth Hormone (GH) and is structurally homologous to Proinsulin. The 7.6 kDa mature IGF-I is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF-I shares 94% and 96% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively. The body growth of animals is regulated by growth hormone and IGF-I. The classical theory of this regulation is that most IGF-I in the blood originates in the liver and that body growth is controlled by the concentration of IGF-I in the blood. Meanwhile, IGF-I has been shown to enhance neuronal survival and inhibit apoptosis. IGF-1 promote the proliferation of multiple myeloma (MM) cells and protect them against dexamethasone (Dex)-induced apoptosis.   Product Properties Synonyms Somatomedin C, IGF-I, IGF-IA, Mechano growth factor, MGF Accession P05017 GeneID 16000 Source E.coli-derived mouse IGF-1 protein, Gly49-Ala118. Molecular Weight Approximately 7.7 kDa. AA Sequence GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKAA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0×105 IU/mg. Fully biologically active when comparedto standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL- 28A (Interferon-lambda 2; IFN-lambda 2), IL-28B/IFN-lambda 3, and IL-29/IFN-lambda 1 are type III interferons which are distantly related to IL-10 family and type I IFN family cytokines. Mature human IL-28A is an approximately 22-25 kDa protein that shares 66% amino acid (aa) sequence identity with mouse and rat IL-28A and shows cross-species activity. It shares 96% and 70% aa sequence identity with human IL-28B and IL-29, respectively. Type III interferons are upregulated in response to viral infection, and they act predominantly on epithelial cells through a receptor complex that contains IL-10 R beta and IL-28 R alpha /IFN-gamma R1. Type III IFNs function as anti-viral molecules and induce the upregulation of MHC class I antigen. IL-28A promotes the Th1 polarization of dendritic cells in the airway (e.g. production of IL-12 p70 and IFN-gamma ) and inhibits Th2 and Th17 mediated inflammation. In the liver, however, the IL-28A induced Th1 cytokine response contributes to inflammation in T cell mediated hepatitis. IL-28A additionally exhibits anti-tumor activity, in part by enhancing IL-12 dependent anti-tumor CTL responses in vivo. In contrast, it is up-regulated in invasive bladder cancer where it promotes tumor cell migration   Product Properties Synonyms Interleukin 28A；Interferon lambda-2；Interleukin-28A；IFN-lambda-2 Accession Q4VK74 GeneID 330496 Source E.coli-derived Mouse IFN-λ2/IL-28A, Asp20-Val193 Molecular Weight Approximately 19.7 kDa. AA Sequence DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKDAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENMTDS ALATILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFRLL TRDLKCVASG DQCV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by an anti-viral assay usinghuman HepG2 cells infected with encephalomyocarditis is less than 3 ng/ml, corresponding to a specificactivity of > 3.3 × 105 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, with 5 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL-28B (also named interferon-lambda 3, IFN-lambda 3), IL-28A (IFN-lambda 2) and IL-29 (IFN-lambda 1) are type III interferons that are class II cytokine receptor ligands. They are distantly related to members of the IL-10 family and type I IFN family. Human IL-28B cDNA encodes a 200 amino acid (aa) protein with a 25 aa signal peptide and a 175 aa mature protein that lacks N-glycosylation sites. Mature human IL-28B shares 64% and 75% aa sequence identity with mouse and canine IL-28B, respectively, and is active across species. Human IL-28B shares 94% and 69% aa identity with human IL-28A and IL- 29, respectively. Type III interferons are widely expressed, but are mainly produced by antigen presenting cells in response to viruses  and double-stranded RNA that interact with Toll-like receptors or RIG-1 family helicases. They signal through a widely expressed receptor that is a heterodimer of the IL-10 receptor beta (IL-10 R beta ) and IL-28 receptor alpha (IL-28 R alpha ; also called IFN-lambda R1). Interaction of either type I or type III IFNs with their receptors activates similar pathways, including JAK tyrosine kinase activation, STAT phosphorylation and formation of the IFN-stimulated regulatory factor 3 (ISGF-3) transcription factor complex. Both type  I and III IFNs induce anti- viral activity and up- regulate MHC class I antigen expression. Cell lines responsive to type III IFNs are also responsive to type I IFNs, but in general, higher concentrations of type III IFNs are needed for similar in vitro responses. In vivo, however, type III IFNs enhance levels of IFN-gamma in serum, suggesting that the robust anti-viral activity of type III IFNs may  stem in part from activation of the immune system. Anti-proliferative and antitumor activity in vivo has also been shown for type III IFNs.   Product Properties Synonyms Interleukin 28B；Interferon lambda-3；IFN-lambda-3；Interleukin-28B Accession Q8CGK6 GeneID 338374 Source E.coli-derived mouse Interferon-lambda3/Interleukin-28B protein, Asp20-Val193 Molecular Weight Approximately 19.6 kDa. AA Sequence DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKGAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENINDS ALTTILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFQLL LRDLKCVASG DQCV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis is less than 30 ng/ml, corresponding to a specific activity of > 3.3 × 104 IU/mg Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-1 alpha (IL1a) is also known as IL-1A, IL1,and is a cytokine of the interleukin-1 family. Among various species, the amino acid sequence of mature IL-1 alpha is conserved 60% to 70% and human IL-1 has been found to be biologically active on murine cell lines. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. IL-1 is a major immunoregulatory/proinflammatory cytokine which also affects fibroblast proliferation and function and therefore it was of interest to investigate whether its constitutive expression influences the in vivo tumorigenic potential of transformed fibroblastoid cell lines.   Product Properties Synonyms Interleukin-1 alpha, IL-1α, BAF, IL-1F1, LAF, LEM, preinterleukin 1 alpha, pro-interleukin-1-alpha Accession Q3U0Y6 GeneID 16175 Source E.coli-derived mouse IL-1alpha protein, Ser115-Ala270. Molecular Weight Approximately 17.9 kDa. AA Sequence SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 2 pg/mL, corresponding to a specific activity of > 5.0 × 108 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin 16 (IL-16), also known as lymphocyte chemoattractant factor (LCF), refers to the C-terminal peptide of  pro-IL-16 isoform 1, which is a nuclear and cytoplasmic PDZ-containing protein. The C-terminus of pro-IL-16 is cleaved by Caspase-3, resulting in the release of secreted IL-16. Mature IL-16 has been shown to bind the cell surface receptor CD4 and functions as an immunomodulatory cytokine.   Product Properties Synonyms Lymphocyte chemoattractant factor , LCF Accession O54824 GeneID 16170 Source E.coli-derived Mouse IL-16, Ser1205-Ser1322. Molecular Weight Approximately 12.2 kDa. AA Sequence SAASASAASD ISVESKEATV CTVTLEKTSA GLGFSLEGGK GSLHGDKPLT INRIFKGTEQ GEMVQPGDEI LQLAGTAVQG LTRFEAWNVI KALPDGPVTI VIRRTSLQCK QTTASADS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human peripheral T lymphocytes is in a concentration range of 1.0-100 ng/ml. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin 19 (IL-19) is a member of the IL-10 family of cytokines. The IL-10 family is a class II alpha -helical collection of cytokines that contains two groups, a viral homolog and a cellular homolog group. Within the cellular homolog group, there are two additional groupings, one which uses IL-10 R2 as a signal transducing receptor (IL-10, IL-22 and IL-26), and one which uses IL-20 R2 as a signal transducing receptor (IL-19, IL-20 and IL-24). Mouse IL-19 is synthesized as a 176 amino acid (aa) precursor that contains a 24 aa signal sequence and a 152 aa mature region. Based on human studies, it is expected to be secreted as a glycosylated monomer, 35 - 45 kDa in size. IL-19 is unusual in that it contains seven amphipathic helices. Mature mouse IL-19 shares 69% aa sequence identity with the mature human IL-19, and 85% and 68% aa identity to unpublished Genbank sequences for rat and canine IL-19, respectively. Although mouse IL-19 is active on human cells, human IL-19 is not active on mouse cells. IL-19 expression is limited to activated keratinocytes and monocytes, with a possible contribution from B cells. IL-19 binds a receptor  complex consisting of the IL-20 receptor alpha (also known as IL-20 R1) and the IL-20 receptor beta (IL-20 R2). This receptor complex is  also shared by IL-20 and IL-24. Notably, IL-19 is reported to actually bind to IL-20 R2, which is generally considered to be only the signal transducing receptor subunit. Functionally, it has been reported that IL-19 both will and will not induce IL-6 and TNF production by monocytes. It does, however, seem to drive T-helper cell differentiation towards a Th2 response, inducing both IL-10 and production of itself .   Product Properties Synonyms IL-10C; IL19; MDA1 Accession Q8CJ70 GeneID 329244 Source E.coli-derived Mouse IL-19, Leu25-Ala176. Molecular Weight Approximately 17.6 kDa. AA Sequence LRRCLISVDM RLIEKSFHEI KRAMQTKDTF KNVTILSLEN LRSIKPGDVC CMTNNLLTFY RDRVFQDHQE RSLEVLRRIS SIANSFLCVQ KSLERCQVHR QCNCSQEATN ATRIIHDNYN QLEVSSAALK SLGELNILLA WIDRNHLETP AA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human IL-20Rα and human IL-20Rβ co-transfected murine BaF3 pro-B cells is less than 0.8 ng/mL, corresponding to a specific activity of >1.25 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4 , with 3 % Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-21 (IL-21) is an approximately 14 kDa four-helix-bundle cytokine in the family of cytokines that utilize the common gamma chain (gamma c) as a receptor subunit. Mature mouse IL-21 shares 66%, 59%, 58%, and 88% aa sequence identity with mature canine, human, rabbit, and rat IL-21, respectively. It can induce target cells division or proliferation. IL-21 elicits its effect through binding to IL-21R. IL-21 is a type I cytokine whose receptor is expressed on T, B, and NK cells. Within the B cell lineage, IL-21 regulates IgG1 production and cooperates with IL-4 for the production of multiple Ab classes in vivo. IL-21 has a significant influence on the regulation of B cell function in vivo and cooperates with IL-4. Additionally, IL-21 promoted tumor-specific CTL activity and enhanced memory responses to tumor rechallenge.   Product Properties Synonyms CVID11, IL21, IL-21, interleukin 21, Za11 Accession Q9ES17 GeneID 60505 Source E.coli-derived mouse IL-21 protein, His18-Ser146 Molecular Weight Approximately 15.0 kDa. AA Sequence HKSSPQGPDR LLIRLRHLID IVEQLKIYEN DLDPELLSAP QDVKGHCEHA AFACFQKAKL KPSNPGNNKT FIIDLVAQLR RRLPARRGGK KQKHIAKCPS CDSYEKRTPK EFLERLKWLL QKMIHQHLS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human N1186 T cells is less than 25 ng/mL, corresponding to a specific activity of > 4.0 × 104 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL-33, also known as NF-HEV and DVS 27, is a 17.5 kDa proinflammatory protein that may also regulate gene transcription. DVS  27 was identifed as a gene that is up- regulated in vasospastic cerebral arteries. NF-HEV was described as a nuclear factor that is preferentially expressed in the endothelial cells of high endothelial venules relative to endothelial cells from other tissues. IL-33 was identified based on sequence and structural homology with IL-1 family cytokines. DVS 27, NF-HEV, and IL-33 share 100% amino acid sequence identity. IL-33 is constitutively expressed in smooth muscle and airway epithelia. It is up- regulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL- 1 beta stimulation. Similar to IL-1, IL-33 can be cleaved in vitro by caspase- 1, generating an N- terminal fragment that is slightly shorter than the C- terminal fragment. The N- terminal portion of full length IL-33 contains a predicted bipartite nuclear localization sequence and a homeodomain-like helix-turn-helix DNA binding domain. By immunofluorescence, full length IL-33 localizes to the nucleus in HUVECs and transfectants. The C- terminal fragment, corresponding to mature IL-33, binds and triggers signaling through mast cell IL- 1 R4/ST2L, a longtime orphan receptor involved in the augmentation of Th2 cell responses. A ternary signaling complex is formed by the subsequent association of IL-33 and ST2L with IL- 1 RAcP. Stimulation of Th2 polarized lymphocytes with mature IL-33 in vitro  induces  IL-5  and  IL-13  secretion. In vivo administration of mature IL-33 promotes increased production of IL-5, IL-13, IgE, and IgA, as well as splenomegaly and inflammatory infiltration of mucosal tissues. Full length and mature mouse IL-33 share approximately 55% and 90% aa sequence identity with human and rat IL-33, respectively. Mouse IL-33 shares less than 25% aa sequence identity with other IL-1 family proteins.   Product Properties Synonyms IL-1F11, NF-HEV Accession Q8BVZ5 GeneID 77125 Source E.coli-derived Mouse IL-33, Ser109-Ile266. Molecular Weight Approximately 17.5 kDa. AA Sequence SIQGTSLLTQ SPASLSTYND QSVSFVLENG CYVINVDDSG KDQEQDQVLL RYYESPCPAS QSGDGVDGKK LMVNMSPIKD TDIWLHANDK DYSVELQRGD VSPPEQAFFV LHKKSSDFVS FECKNLPGTY IGVKDNQLAL VEEKDESCNN IMFKLSKI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, and 1 mM EDTA. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL- 36 alpha, previously called IL- 1F6 and FIL1 epsilon (family of IL- 1 member epsilon), is a member of the IL- 1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, and novel family members IL- 36 Ra (IL- 1F5), IL- 36 beta (IL- 1F8), IL- 36 gamma (IL- 1F9), IL- 37 (IL- 1F7) and IL- 1F10. All family members show a 12 beta - strand, beta - trefoil configuration, and are believed to have arisen from a common ancestral gene. It can be externalized non- specifically in response to LPS and ATP- induced activation of the P2X7 receptor. Full- length recombinant IL- 36 alpha is less active than endogenous IL- 36 alpha, but trimming of the N- termini enhances its activity. Mouse IL- 36 alpha shares 83% aa sequence identity with rat IL- 36 alpha, 54- 60% with human, rabbit, equine and bovine IL- 36 alpha, and 27- 57% aa sequence identity with other novel IL- 1 family members. IL- 36 alpha is mainly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. It is expressed by monocytes, B and T cells. The receptor for IL- 36 alpha is a combination of IL- 1 Rrp2 (also called IL- 1 RL2 or IL- 1 R6), mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL- 36 alpha, beta and gamma all activate NF- kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and induce production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. IL- 36 alpha and other family members are overexpressed in psoriatic skin lesions, and transgenic overexpression of IL- 36 alpha in skin keratinocytes produces epidermal hyperplasia. IL- 36 alpha is present in kidney tubule epithelia; it is highly overexpressed in tubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. IL- 36 alpha is induced by inflammation in adipose tissue- resident alternately activated (M2) macrophages, and reduces adipocyte differentiation.   Product Properties Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Accession Q9JLA2 GeneID 54448 Source E.coli-derived Mouse IL-36α,153aa, Arg8-His160. Molecular Weight Approximately 17.1 kDa. AA Sequence RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing IL-6 secretion in murine NIH/3T3 cells is less than 25 ng/mL, corresponding to a specific activity of > 4.0 × 104 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, 1 mM DTT, 3 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL- 36 alpha, previously called IL- 1F6 and FIL1 epsilon (family of IL- 1 member epsilon), is a member of the IL- 1 family which includes IL- 1 beta, IL- 1 alpha, IL- 1ra, IL- 18, and novel family members IL- 36 Ra (IL- 1F5), IL- 36 beta (IL- 1F8), IL- 36 gamma (IL- 1F9), IL- 37 (IL- 1F7) and IL- 1F10. All family members show a 12 beta - strand, beta - trefoil configuration, and are believed to have arisen from a common ancestral gene. IL- 36 alpha is an 18 kDa, 160 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N- linked glycosylation sites. It can be externalized non- specifically in response to LPS and ATP- induced activation of the P2X7 receptor. Full- length recombinant IL- 36 alpha is less active than endogenous IL- 36 alpha, but trimming of the N- termini enhances its activity. Mouse IL- 36 alpha shares 83% aa sequence identity with rat IL- 36 alpha, 54- 60% with human, rabbit, equine and bovine IL- 36 alpha, and 27- 57% aa sequence identity with other novel IL- 1 family members. IL- 36 alpha is mainly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. It is expressed by monocytes,  B and T cells. The receptor for IL- 36  alpha is a combination of IL- 1  Rrp2 (also called     IL- 1 RL2 or IL- 1 R6), mainly found in epithelia and keratinocytes, and the widely expressed IL- 1 RAcP. IL- 36 alpha, beta and gamma all activate NF- kappa B and MAPK pathways in an IL- 1 Rrp2 dependent manner, and induce production of inflammatory cytokines and chemokines such as CXCL8/IL- 8. IL- 36 alpha and other family members are overexpressed in psoriatic skin lesions, and transgenic overexpression of IL- 36 alpha in skin keratinocytes produces epidermal hyperplasia. IL- 36 alpha is present in kidney tubule epithelia; it is highly overexpressed in tubulointerstitial lesions in mouse models of chronic glomerulonephritis, lupus nephritis and diabetic nephritis. IL- 36 alpha is induced by inflammation in adipose tissue- resident alternately activated (M2) macrophages, and reduces adipocyte differentiation.   Product Properties Synonyms FIL1 epsilon, IL-1 epsilon, IL-1F6, IL-1H1 Accession Q9JLA2 GeneID 54448 Source E.coli-derived Mouse IL-36α,160aa, Met1-His160, with an N-terminal Met. Molecular Weight Approximately 18.0 kDa. AA Sequence MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The specific activity determined by its ability in a functional ELISA. Immobilized rMuIL-36α at 1 µg/mL can bind recombinant murine IL-1 Rrp2 with a range of 0.15-5 µg/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 5 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Mouse interleukin-36 beta [IL-36 beta ; previously IL-1F8, FIL-1 eta(eta) and IL-1H2] is a member of the IL-1 family  of proteins that includes IL-1 beta, IL-1 alpha, IL-1ra, IL-18, IL-36Ra/IL-1F5, IL-36 alpha /IL-1F6, IL-37/IL-1F7, IL-36 gamma /IL-1F9 and IL-1F10. All family members show a 12 beta-stranded beta-trefoil configuration, share up to 50% amino acid (aa) sequence identity, and are believed to have arisen from a common ancestral gene. Although two alternatively spliced transcript variants for human  IL-36 beta /IL-1F8 have been described, to date, only one mouse IL-36 beta /IL-1F8 isoform is known. Mouse IL-36 beta /IL-1F8 shares 61% and 74% aa identity with human IL-36 beta isoform 2 and rat IL-36 beta, respectively. IL-36 beta is agonistic, stimulating release of inflammatory mediators such as IL-6 and IL-8, and cytotoxic peptides such as beta-defensins 2 and 3 that aid in defense against microbial pathogens. The receptor for IL-36 proteins is IL-1 Rrp2, with IL-1 RAcP as a coreceptor. Antagonism of IL-36 proteins by IL-36Ra, which also binds IL-1 Rrp2, has been shown by some investigators. Skin keratinocytes express highest levels of IL-36 proteins and their receptors, followed by epithelia in the esophagus, trachea and bronchae. IL-36 beta expression is increased in psoriatic skin and may play a role in pathogenesis of psoriasis. IL-36 beta is also expressed in resting and activated monocytes and B cells, synovial fibroblasts, neurons and glia, and is detectable in plasma and body fluids. IL-36 beta, along with IL-36 alpha and  IL-36 gamma, is up-regulated by IL-1 alpha and TNF- alpha in keratinocytes, and has been shown to activate NF- kappa B and MAPK signaling pathways in an IL-1 Rrp2-dependent manner. Full-length recombinant IL-36 proteins appear less active than their endogenous counterparts, but trimming of the N-termini enhances their activity.   Product Properties Synonyms FIL1 eta, IL-1 eta, IL-1F8, IL-1H2 Accession Q9D6Z6 GeneID 69677 Source E.coli-derived Mouse IL-36β, 153aa, Ser31-Lys183. Molecular Weight Approximately 17.4 kDa. AA Sequence SSQSPRNYRV HDSQQMVWVL TGNTLTAVPA SNNVKPVILS LIACRDTEFQ DVKKGNLVFL GIKNRNLCFC CVEMEGKPTL QLKEVDIMNL YKERKAQKAF LFYHGIEGST SVFQSVLYPG WFIATSSIER QTIILTHQRG KLVNTNFYIE SEK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing IL-6 secretion in murine NIH/3T3 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 5 % trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CXCL10 is a cytokine belonging to the CXC chemokine family. Mouse CXCL10 shares approximately 67% amino acid sequence identity with human CXCL10. CXCL10 has been shown to be a chemoattractant for activated T-lymphocytes and monocytes. It also has the effect of promoting the adhesion of T cells to endothelial cells, as well as inhibiting bone marrow colony formation and angiogenesis.   Product Properties Synonyms Gamma-IP10, Small-inducible Cytokine B10, C7, CXCL10, gIP-10, IFI10, Interferon-gamma Induced Protein CRG-2 Accession P17515 GeneID 15945 Source E.coli-derived mouse IP-10/CXCL10 protein, Ile22-Pro98. Molecular Weight Approximately 8.7 kDa. AA Sequence IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity The biologically active determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 0.1-10.0 ng/mL in the presence of IL-2.   Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Monocyte colony-stimulating factor (M-CSF) is a macrophage lineage-specific growth factor. M-CSF Induces vascular endothelial growth factor production and angiogenic activity from human monocytes. Whatmore, M-CSF and GM-CSF are mediators involved in regulating the numbers and function of macrophage lineage populations and have been shown to contribute to macrophage heterogeneity.   Product Properties   Synonyms CSF-1, MGI-IM, MCSF, M-CSF, MGC31930 Source Recombinant Mouse M-CSF is expressed from Yeast with N-His. It contains Lys33-Glu262. Endotoxin < 1.0 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4), with 1%BSA. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS,with 1%BSA.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Description NGF was discovered as a molecule that promoted the survival and differentiation of sympathetic and sensory neurons in the peripheral nervous system.NGF is the first member discovered in the Neurotrophin family, which includes brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4).   Product Properties Synonyms beta Nerve Growth Factor; Ngfb Uniprot No. NP_001106168.1 Source Recombinant Mouse NGF Protein is expressed from CHO Stable Cells Cells with an initial Met at the C-terminus. It contains Ser 122-Gly 241. Molecular Weight The recombinant mouse NGF has a calculated molecular mass of 13.5 kDa as estimated in SDS-PAGE under reducing conditions. Biological Activity Measured in a cell proliferation assay using  TF-1  human  erythroleukemic  cells.  The  ED50 for this effect is 1-6 ng/mL. Purity > 95% as determined by SDS-PAGE. Endotoxin <1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from sterile 150mM NaCl, 50mM NaAc, pH 5.5.Normally 5% - 8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring  the  contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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