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PlGF-2 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-2 is expressed in umbilical vein endothelial cells and placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-2 also signals through Neuropilin (NP-1), and can bind with high affinity to heparin. Recombinant Human PlGF-2 is a 34.6 kDa disulfide-linked homodimeric protein of two 152 amino acid polypeptide chains.   Product Properties   Synonyms Placenta Growth Factor-2, PGFL Accession P49763-3 GeneID 5228 Source E.coli-derived Human PlGF-2 protein,Leu19-Arg131. Molecular Weight Approximately 34.6 kDa. AA Sequence LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active as determined by its ability to chemoattract human monocytes using a concentration range of 5.0-50 ng/mL. 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 0.02 % 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.   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.   Caution   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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CXCL4, also called PF4 (platelet factor 4), is an 8 kDa member of the CXC chemokine family, sharing features with CXCL8/IL-8 and CXCL7/NAP-2. Mature human CXCL4 shares 65-76% amino acid sequence identity with mouse, rat, bovine, ovine and porcine CXCL4. The active protein is a tetramer of CXCL4 subunits that forms a ring of heparin-binding positive charges from sites at the C-terminal region of each monomer. Megakaryocytes synthesize CXCL4 and store it in platelet alpha -granules. Secretion from activated platelets can produce micromolar levels in serum and over 100-fold higher within clots. In contrast to other CXC chemokines, CXCL4 does not contain an ELR motif and lacks binding to nearly all chemokine receptors. A potential high-affinity G-protein-coupled receptor for CXCL4, the CXCR3 isoform CXCR3B, is expressed in human but not mouse. In most cases, it is likely that cell surface binding and signaling properties of CXCL4 are due to binding of glycosaminoglycans chains, particularly chondroitin sulfates. CXCL4 released from activated platelets binds and regulates thrombin/thrombomodulin complexes, regulates and enhances production of activated Protein C (APC), and limits the coagulation cascade. It binds and influences the enzymatic activity of coagulation factor Xa. It binds fibrin and affects clot structure. Therapeutic doses of the anticoagulant heparin neutralize CXCL4 procoagulant effects.   Product Properties   Synonyms Iroplact, Oncostatin-A Accession P02776 GeneID 5196 Source E.coli-derived Human GRO-γ,Glu32-Ser101. Molecular Weight Approximately 7.8 kDa AA Sequence EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% 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 fibroblasts is in a concentration of 1.0-10 ng/mL. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in Acetonitrile and 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 °C. Further dilutions should be made in appropriate buffered solutions.   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.   Caution   1. Avoid repeated freeze-thaw cycle. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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PTN was identified independently by several groups as a novel heparin-binding, developmentally regulated cytokine. Depending on the biological activities studied, this protein has variously been referred to as heparin-binding brain mitogen (HBBM), heparin-binding growth factor-8 (HBGF-8), heparin-binding neurite promoting factor, heparin-binding neurotrophic factor (HBNF),  heparin-affinity regulatory peptide (HARP), heparin-binding growth-associated molecule (HB-GAM), osteoblast-specific factor  (OSF-1), and pleiotrophin. PTN is a highly conserved protein; the amino acid sequences of human, bovine, rat, and mouse PTN share > 98% homology.PTN is a member of a family of heparin-binding proteins that share sequence, structural, and functional similarity. Other members of this family include midkine (MK), and chicken retinoic acid-induced heparin-binding protein (RI-HB), an avian homologue of MK. The expression of all these cytokines is restricted and highly regulated during development. PTN can be  used as an attachment substrate to stimulate neurite outgrowth in mixed cultures of embryonic rat, mouse or chicken brain cells.  Although both natural and recombinant human PTN have been reported to be mitogenic for fibroblasts, endothelial, and epithelial cells, the data are still highly controversial.   Product Properties   Synonyms HARP; HBBM; HB-GAM; HBGF8; HBNF Accession P21246 GeneID 5764 Source E.coli-derived human PTN, Gly33-Asp168. Molecular Weight Approximately 15.3 kDa. AA Sequence GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity was measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons, when neurons were plated on 96 well culture plates that had been pre-coated with 100 µl/well of a solution of 5-10 µg/mL rHuPTN. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by 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.   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.   Caution   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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This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants. Product Properties   Synonyms Human Proinsulin C-Peptide Analogue, IDDM Protein, Human; IDDM1 Protein, Human Accession P01308 GeneID 3630 Source E.coli-derived human Proinsulin C-Peptide Analogue protein,Arg55-Arg89 Molecular Weight Approximately 3.6 kDa. AA Sequence RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 0.1 EU/μg of the protein as determined by 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.   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.   Caution   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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Kallikrein 3, commonly known as prostate specific antigen (PSA), is a serine protease of the human tissue Kallikrein gene family. The human tissue kallikrein (KLK) gene family contains 15 members that play important roles in cancer. Kallikrein-3, called prostate specific antigen (PSA), is a glycoprotein enzyme encoded in humans by the KLK3 gene. PSA is secreted by the epithelial cells of the prostate gland, hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. PSA is an established tumor marker that aids in the diagnosis, staging, and follow up of prostate cancer.   Product Properties   Synonyms APS seminin, hK3, Kallikrein 3, KLK2A1, KLK3, P-30 antigen, PSA Accession P07288 GeneID 354 Source E.coli-derived human PSA/Kallikrein-3 protein, Ile25-Pro261. Molecular Weight Approximately 26.1 kDa. AA Sequence IVGGWECEKH SQPWQVLVAS RGRAVCGGVL VHPQWVLTAA HCIRNKSVIL LGRHSLFHPE DTGQVFQVSH SFPHPLYDMS LLKNRFLRPG DDSSHDLMLL RLSEPAELTD AVKVMDLPTQ EPALGTTCYA SGWGSIEPEE FLTPKKLQCV DLHVISNDVC AQVHPQKVTK FMLCAGRWTG GKSTCSGDSG GPLVCNGVLQ GITSWGSEPC ALPERPSLYT KVVHYRKWIK DTIVANP 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 biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl, 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.   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.   Caution   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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RANTES is a CC chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant Human RANTES is a 7.8 kDa protein containing 68 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines.   Product Properties   Synonyms SIS-delta, Small-inducible cytokine A5, T-cell-specific protein RANTES Accession P13501 GeneID 6352 Source E.coli-derived Human CCL5 protein,Ser24-Ser91. Molecular Weight Approximately 7.8 kDa. AA Sequence SPYSSDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS 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 monocytes is in a concentration range of 1.0-10 ng/mL. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PB, pH 7.4, 100 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°C. Further dilutions should be made in appropriate buffered solutions.   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.   Caution   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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Rb encoded by the RB1 gene in humans, is expressed by retina and belongs to the etinoblastoma-associated protein family. The hole protein consists of 928 a.a. and the rHuRb fragment occupies sequence of 792-929 a.a.. Rb is a key regulator of entry into cell division that acts as a tumor suppressor. It has many functions, for example, promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C, and acts as a transcription repressor of E2F1 target genes and so on. The rHuRb is the region that rich of modified residue like phosphothreonine and N6-acetyllysine. Product Properties   Synonyms p105-Rb, pRb, pp110 Accession Q59HH0 GeneID 4595173 Source E.coli-derived human Rb137 protein, Phe792-Lys928. Molecular Weight Approximately 16.5 kDa. AA Sequence MASFPSSPLR IPGGNIYISP LKSPYKISEG LPTPTKMTPR SRILVSIGES FGTSEKFQKI NQMVCNSDRV LKRSAEGSNP PKPLKKLRFD IEGSDEADGS KHLPGESKFQ QKLAEMTSTR TRMQKQKMND SMDTSNKEEK HHHHHH Tag C-His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 1.0 EU/μg of the protein as determined by 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.   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.   Caution   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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Human RSPO1 protein, also known as R-Spondin 1, is a naturally occurring protein in the human body that plays a significant role in the Wnt signaling pathway. This pathway regulates various cellular functions, including cell growth, differentiation, and tissue regeneration. RSPO1 acts as an agonist, meaning it enhances the activity of Wnt proteins by binding to their receptors and activating them. This activation leads to downstream signaling events that impact cell behavior and tissue development.   Product Properties Synonyms   R-Spondin 1；Roof Plate-specific Spondin 1   Uniprot No.  Q2MKA7 Source E.coli-derived human RSPO1 protein, Arg21-Ala263，with N-terminal His tag. Molecular Weight Approximately 27.6 kDa. Purity > 50% as determined by SDS-PAGE. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Liquid in 20 mM Tris，1 M NaCl，pH8.0，the concentration is 0.05 mg/ml.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 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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S100B is a member of the S100 family of proteins containing two EF-hand-type calcium-binding motifs. S100B exerts both  intracellular and extracellular functions. Intracellular S100B acts as a stimulator of cell proliferation and migration and an inhibitor of apoptosis and differentiation, which might have important implications during brain, cartilage and skeletal muscle development and repair, activation of astrocytes in the course of brain damage and neurodegenerative processes, and of cardiomyocyte remodeling after infarction, as well as in melanomagenesis and gliomagenesis. As an extracellular factor, S100B engages RAGE (receptor for advanced glycation end products) in a variety of cell types with different outcomes (i.e. beneficial or detrimental, pro-proliferative or pro-differentiative) depending on the concentration attained by the protein, the cell type and the microenvironment. This calcium binding astrocyte-specific cytokine, presents a marker of astrocytic activation and reflects CNS injury. The excellent sensitivity of S100B has enabled it to confirm the existence of subtle brain injury in patients with mild head trauma, strokes, and after successful resuscitation from cardiopulmonary arrest. Recent findings provide evidence, that S100B may decrease neuronal injury and/or contribute to repair following traumatic brain injury (TBI). Hence, S100B, far from being a negative determinant of outcome, as suggested previously in the human TBI and ischemia literature, is of potential therapeutic value that could improve outcome in patients who sustain various forms of acute brain damage.   Product Properties   Synonyms NEF Protein, Human; S100 Protein, Human; S100-B Protein, Human; S100beta Protein, Human Accession P04271 GeneID 6285 Source E.coli-derived Human S100B protein,Ser2-Glu92 Molecular Weight Approximately 10.6 kDa. AA Sequence SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDG DGECDFQEFMAFVAMVTTACHEFFEH E Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % 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 monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm 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.   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.   Caution   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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CD40 Ligand, also known as TNFSF, a type II membrane protein with homology to TNF, is transiently expressed on activated T cells and known to be important for B cell Ig production and for activation and differentiation of monocytes and dendritic cells. Mature human CD40 Ligand consists of a 22 amino acid (aa) cytoplasmic domain, a transmembrane segment, and an 215 aa extracellular region . It is primarily expressed on activated CD4+ T lymphocytes, and also found in other types of cells, like NK cells, mast cells, basophils and eosinophils. In total CD40 ligand has three binding partners: CD40, α5β1 integrin and αIIbβ3. CD40 Ligand dysregulation on T cells and antigen presenting cells contributes to the immune deficiency associated with HIV infection and AIDS. CD40 ligation by CD40 Ligand promotes B cell activation and T cell-dependent humoral responses.   Product Properties   Synonyms CD154 antigen, CD154, CD40 antigen ligand, CD40 Ligand, gp39, HIGM1, T-B cell-activating molecule, T-BAM, TNFSF5, TNFSF5IMD3, TRAP Accession P29965 GeneID 959 Source E.coli-derived human sCD40L protein, Met113-Leu261. Molecular Weight Approximately 16.3 kDa. AA Sequence MQKGDQNPQI AAHVISEASS KTTSVLQWAE KGYYTMSNNL VTLENGKQLT VKRQGLYYIY AQVTFCSNRE ASSQAPFIAS LWLKSPGRFE RILLRAANTH SSAKPCGQQS IHLGGVFELQ PGASVFVNVT DPSQVSHGTG FTSFGLLKL 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 the dose-dependent stimulation of IL-8 production by human PBMC is less than 5-10 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PBS, pH 7.0. 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.   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.   Caution   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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SCF, also known as stem cell factor or kit ligand, is a cytokine that plays a critical role in the survival, proliferation, and differentiation of hematopoietic stem cells and early progenitor cells. SCF is primarily produced by bone marrow stromal cells and functions by binding to the c-kit receptor on the surface of hematopoietic cells. Dysregulation of SCF signaling has been implicated in various types of cancer and hematological disorders.   Product Properties   Synonyms KITLG; FPH2; KL-1; Kitl; MGF; SF; SHEP7; KL Accession P21583-1 Source Recombinant Human SCF Protein is expressed from E.coli without tag. It contains Glu26-Ala189 Molecular Weight Approximately 18.45 kDa. Tag None Purity > 95% by SDS-PAGE and HPLC analyses. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization. Reconstitution Centrifuge the tube before opening, Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.   Storage   The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 -6 months, -85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   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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Secreted protein acidic and rich in cysteine (SPARC), also named as osteonectin or BM-40, is an acronym for “secreted protein, acidic and rich in cysteine”. Mature human SPARC shows 92%, 92%, 97%, 99%, 96% and 85% aa identity with mouse, rat, canine, bovine, porcine and chick SPARC. SPARC is the founding member of a family of secreted matricellular proteins with similar domain structure. It is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion.   Product Properties   Synonyms Basement-membrane Protein 40, BM-40, Osteonectin, ON, SPARC Accession P09486 GeneID 6678 Source E.coli-derived human SPARC protein, Ala18-Asp1303. Molecular Weight Approximately 32.7 kDa. AA Sequence APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 99 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is less than 3.0 μg/mL, corresponding to a specific activity of > 333 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by 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.   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.   Caution   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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  Name Catalog No. Size Recombinant Human SLC1A5 Full Length Protein (VLP) C230780E 20 μg C230780S 100 μg C230780M 100 μg C230780L 1 mg   Product Properties   Synonyms SLC1A5 / AAAT / ASCT2 / M7V1 / RDR / RDRC Source HEK293 Cells AA sequence Accession #Q15758: Met1 - Met541 Endotoxin < 1EU per μg by the LAL method. Purity >95% as determined by DLS. Formulation 115mM Gly 4% trehalose Activity ELISA：Immobilized Human SLC1A5 VLP at 5 ug/mL (30 uL/well) can bind idactamab (P100098) , The EC50 was approximately 0.004176 ug/ml. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Figure Figure 1. Immobilized Human SLC1A5 VLP at 5 ug/mL (30 uL/well) can bind idactamab (P100098) , The EC50 was approximately 0.004176 ug/ml. Storage The product should be stored at -85~-65℃ 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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  Name Catalog No. Size Recombinant Human SLC7A11 Protein-VLP C230752E 20 μg C230752S 100 μg C230752M 100 μg C230752L 1 mg   Product Properties   Synonyms (Amino acid transport system xc-)(Calcium channel blocker resistance protein CCBR1)(Solute carrier family 7 member 11)(xCT) Source HEK293 Cells AA sequence Accession #Q9UPY5: Met1 - Leu501 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ 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.        This product is for research use only.   

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Fas and Fas Ligand (FasL) belong to the TNF superfamily, and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and a 145 amino acid cytoplasmic domain. Recombinant Human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR-homologous cysteine-rich extracellular Fas domain. Product Properties   Synonyms TNFRSF6, CD95, Apo I, Fas Antigen Accession P25445 GeneID 355 Source E.coli-derived Human sFasR/TNFRSF6 protein,Arg17-Asn173. Molecular Weight Approximately 17.6 kDa. AA Sequence RLSSKSVNAQ VTDINSKGLE LRKTVTTVET QNLEGLHHDG QFCHKPCPPG ERKARDCTVN GDEPDCVPCQ EGKEYTDKAH FSSKCRRCRL CDEGHGLEVE INCTRTQNTK CRCKPNFFCN STVCEHCDPC TKCEHGIIKE CTLTSNTKCK EEGSRSN 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 its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/mL in the presence of 2 ng/mLof rHuFas Ligand. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 20 mM PB, pH 7.4, 150 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°C. Further dilutions should be made in appropriate buffered solutions.   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.   Caution   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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TNF receptor 1 (TNF RI; also called TNF R-p55/p60 and TNFRSF1A) is a 55 kDa type I transmembrane protein member of the TNF receptor superfamily, designated TNFRSF1A. Human TNF RI is a 455 amino acid (aa) protein that contains a 21 aa signal sequence and 190 aa ECD with a PLAD (pre-ligand assembly domain) that mediates constitutive dimer/trimer formation, followed by four CRD (cysteine-rich domains), a 23 aa transmembrane domain, and a 221 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain. The ECD of human TNF RI shows 70%, 69%, 80%, 80%, and 73% aa identity with mouse, rat, canine, feline and porcine TNF RI, respectively; and it shows 23% aa identity with the ECD of TNF RII. Both TNF RI and TNF RII (TNFRSF1B) are widely expressed and contain four TNF-alpha trimer-binding CRD in their ECD. However, TNF RI is thought to mediate most of the cellular effects of TNF-alpha. It is essential for proper development of lymph node germinal centers and Peyer's patches, and for combating intracellular pathogens such as Listeria. TNF RI is also a receptor for TNF-beta /TNFSF1B (lymphotoxin-alpha ). TNF RI is stored in the Golgi and translocates to the cell surface following pro-inflammatory stimuli. TNF-alpha stabilizes TNF RI and induces its sequestering in lipid rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE. Product Properties   Synonyms Human sTNF RI Accession P19438 GeneID 7132 Source E.coli-derived Human sTNF RI protein,Ile22-Thr211. Molecular Weight Approximately 17.6 kDa. AA Sequence IYPSGVIGLV PHLGDREKRD SVCPQGKYIH PQNNSICCTK CHKGTYLYND CPGPGQDTDC RECESGSFTA SENHLRHCLS CSKCRKEMGQ VEISSCTVDR DTVCGCRKNQ YRHYWSENLF QCFNCSLCLN GTVHLSCQEK QNTVCTCHAG FFLRENECVS CSNCKKSLEC TKLCLPQIEN VKGTEDSGTT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the TNF-alpha mediated cytotoxicity in the L-929 cells is less than 0.05 μg/mL, corresponding to a specific activity of > 2 × 10 4IU/mg in the presence of 0.25 ng/mL of rHuTNF-alpha. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm 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.   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.   Caution   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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TNF RII (Tumor Necrosis Factor Receptor II), also known as TNFRSF1B, p75/p80, and CD120b, is a widely expressed receptor for membrane-associated TNF-alpha and Lymphotoxin-alpha. Its activation initiates pro-inflammatory and pro-survival responses via NFkB-dependent signaling pathways, although it may also induce apoptosis. Product Properties   Synonyms Human sTNF RII Accession P20333 GeneID 7133 Source E.coli-derived Human sTNF RI protein,Ile22-Thr211. Molecular Weight Approximately 20.0kDa. AA Sequence MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the TNF-α mediated cytotoxicity in the L-929 cells is less than 0.2 μg/mL, corresponding to a specific activity of > 5000 IU/mg in the presence of 0.25 ng/mL of rHuTNF-α. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm 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.   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.   Caution   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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Shh (Sonic Hedgehog protein) is a signaling molecule and a member of the Hedgehog (Hh) family. It plays a crucial role in physiological processes such as embryonic development, tissue regeneration, and cell proliferation. The Shh protein activates the Hh signaling pathway by binding to its receptor Patched (Ptch), which in turn activates the G protein-coupled receptor Smoothened (Smo). This signaling pathway is involved in the directed development of various organs and tissues during embryogenesis, including the central nervous system, limbs, and cardiovascular system. Due to the importance of Shh protein in development and tissue repair, it is also widely studied for its applications in stem cell culture, tissue engineering, and drug development. This recombinant human Shh is provided in the form of lyophilized powder, with high activity, high purity, low endotoxin, and without any additional tags. Product Properties   Synonyms HHG1, HHG-1, HLP3, HPE3, MCOPCB5 Accession Q15465 Source E.coli-derived Human shh, Cly25-Gly197, with an N-terminal Met. Molecular Weight Approximately 19.8kDa. AA Sequence IVIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEE SLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSVAAKSGG 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 inducing alkaline phosphatase production of murine C3H/10T1/2 cells is less than 1 μg/mL, corresponding to a specific activity of > 1.0 × 103 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 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°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at-25~-15℃  for 1 year. 7 days, 2 to 8 °C under sterile conditions after reconstitution.  3 months,-85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   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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Sox2 belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and the determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development, including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4 into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in their capacity to form teratomas in immune-deficient mice. Sox2 and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Product Properties   Synonyms SOX2-TAT Accession P48431 GeneID 6657 Source E.coli-derived Human SOX2-TAT, Met1-Met317, with an N-terminal Met. Molecular Weight Approximately 36.0kDa. AA Sequence MYNMMETELK PPGPQQTSGG GGGNSTAAAA GGNQKNSPDRVKRPMNAFMVWSRGQRRKMA QENPKMHNSE ISKRLGAEWK LLSETEKRPF IDEAKRLRAL HMKEHPDYKYRPRRKTKTLM KKDKYTLPGG LLAPGGNSMA SGVGVGAGLG AGVNQRMDSY AHMNGWSNGS YSMMQDQLGY PQHPGLNAHG AAQMQPMHRY DVSALQYNSM TSSQTYMNGS PTYSMSYSQQ GTPGMALGSM GSVVKSEASS SPPVVTSSSH SRAPCQAGDL RDMISMYLPG AEVPEPAAPS RLHMSQHYQS GPVPGTAING TLPLSHMGGY GRKKRRQRRR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 1.0 EU/μg of the 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.   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.   Caution   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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RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK+ T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage.   Product Properties   Synonyms soluble Receptor Activator of NF-κB Ligand, TNFSF11, TRANCE (TNF-related activation-induced cytokine), OPGL, ODF Accession O14788 Source HEK293 Cells-derived human sRANKL protein, Gly64-Asp24 Molecular Weight Approximately 20.5 kDa. AA Sequence VALFFYF RAQMDPNRIS EDGTHCIYRI LRLHENADFQ DTTLESQDTK LIPDSCRRIK QAFQGAVQKE LQHIVGSQHI RAEKAMVDGS WLDLAKRSKL EAQPFAHLTI NATDIPSGSH KVSLSSWYHD RGWAKISNMT FSNGKLIVNQ DGFYYLYANI CFRHHETSGD LATEYLQLMV YVTKT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 85 % by SDS-PAGE  analyses. Biological Activity 1. Immobilized human TNFSF11 at 2 μg/ml (100 μL/well) can bind human Osteoprotegerin hFc, the EC50 of human Osteoprotegerin hFc is 5-40 ng/mL. 2. The bioactivity of hRANKL was determined by measuring the ability of hRANKL to induce TRAP activity in Raw 264.7 cells. The ED50 for this effect is typically 1.5-7.5 ng/mL. Endotoxin Less than 1.0 EU/μg of the protein as determined by 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.   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.   Caution   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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  Name Catalog No. Size Recombinant Human SSR1 Protein-VLP C230753E 20 μg C230753S 100 μg C230753M 100 μg C230753L 1 mg   Product Properties   Synonyms Translocon-associated protein subunit alpha;SSR1; TRAPA; Translocon-associated protein subunit alpha; TRAP-alpha; Signal sequence receptor subunit alpha; SSR-alpha Source HEK293 Cells AA sequence Accession #P30872:Met1 - Leu391 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ 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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TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-2/DR5 is a 14.9 kDa protein (133 amino acid residues) consisting of the TNFR-homologous, cysteine-rich portion of the extracellular domain.   Product Properties   Synonyms soluble TRAIL Receptor-2, DR5, TNFRSF10B, KILER, TRICK2A, TRICKB Accession O14763 GeneID 8795 Source E.coli-derived Human soluble TRAIL Receptor-2 protein,Glu52-Ser183. Molecular Weight Approximately 14.8 kDa. AA Sequence ESALITQQDL APQQRAAPQQ KRSSPSEGLC PPGHHISEDG RDCISCKYGQ DYSTHWNDLL FCLRCTRCDS GEVELSPCTT TRNTVCQCEE GTFREEDSPE MCRKCRTGCP RGMVKVGDCT PWSDIECVHK ES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. rHusTRAIL-R2 reduced the production of LPS-induced TNF by its ability to neutralize endogenous TRAIL in fresh human PBMC. In this assay, endogenous TRAIL is induced during a 24 hour exposure to LPS (10 ng/mL) but in the presence of rHusTRAIL-R2, TRAIL-induced TNF is suppressed. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PBS, pH 7.0. 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.   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.   Caution   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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CXCL12, also known as SDF-1, is a heparin-binding member of the CXC (or alpha-) family of chemokines. SDF-1 alpha and SDF-1 beta are the first cytokines initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. These proteins were subsequently also cloned from a human stromal cell line. CXCL12β is synthesized as a 93 amino acid (aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region. The mature molecule exhibits a typical three antiparallel beta -strand chemokine-like fold. There are no potential N-linked glycosylation sites.The C-terminus is likely associated with heparin binding . SDF-1 beta circulates and undergoes proteolytic processing. CD26 will remove the first two N-terminal amino acids, possibly creating a reduced-activity chemokine. On the cell surface, the receptor for this chemokine is CXCR4 and syndecan4. Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning and cell number of neural progenitors, and promote angiogenesis. It also enhances the survival of myeloid progenitor cells.   Product Properties   Synonyms hSDF-1 beta, IRH, hIRH, PBSF Accession P48061 GeneID 6387 Source E.coli-derived Human SDF-1β/CXCL12β, Lys22-Met93. Molecular Weight Approximately 8.5 kDa. AA Sequence KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM 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 PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 20-80 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by 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.   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.   Caution   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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Human CXCL12 is expressed as five isoforms that differ only in the C-terminal tail. The gamma isoform of CXCL12, also known as SDF-1 gamma, is a 12 kDa, heparin-binding member of the CXC (or alpha) family of chemokines ,Mature SDF-1 molecules are not glycosylated and exhibit a typical three antiparallel beta -strand chemokine-like fold. N-terminal aa 1 - 8 form a receptor binding site, while aa 1 and 2 (Lys- Pro) are involved in receptor activation. All SDF-1 isoforms can undergo proteolytic processing of the first two N-terminal amino acids by CD26, which is thought to create a reduced- activity chemokine. Human SDF-1 gamma is synthesized as a 119 amino acid (aa) precursor that contains a 21 aa signal sequence and a 98 aa mature region. Mature human SDF-1 gamma shares 99%, 97% and 98% aa identity with mouse, rat, and equine SDF-1 gamma, respectively. The unique C-terminal 26 aa of SDF-1 gamma are highly charged, including four BBXB (where B = basic and X = any aa) motifs, while the most prevalent form, SDF-1 alpha, has 4 unique C-terminal aa and binds heparin via the shared BBXB site more N-terminally located . The SDF- 1 gamma C-terminus binds heparin in secreted SDF-1 gamma, or targets the isoform to the nucleolus in the absence of a signal sequence. SDF-1 isoforms interact with CXCR4 and CXCR7 receptors on the cell surface, and can also bind syndecan-4.   Product Properties   Synonyms CXCL12γ Accession P48061 GeneID 6387 Source E.coli-derived Human CXCL12γ protein,Gly21-Asn119. Molecular Weight Approximately 11.6 kDa. AA Sequence GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/mL. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 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°C. Further dilutions should be made in appropriate buffered solutions.   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.   Caution   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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Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. Human Syndecan-4 ECD shares  approximately 79%, 78% and 81% aa identity with mouse, rat and porcine Syndecan-4 ECD, respectively. Syndecans are the best-characterized plasma membrane proteoglycans with two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. SYND4 is the most similar to SYND2, but is more universally expressed and is found in virtually every cell type. Expression can be upregulated by TGFβ2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator. SYND4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.   Product Properties Synonyms Amphiglycan, MGC22217, Ryudocan, SDC4, syndecan 4, Syndecan4 Accession P31431 GeneID 6385 Source E.coli-derived human SYND4 protein, Glu19-Glu145 Molecular Weight Approximately 13.9 kDa. AA Sequence ESIRETEVID PQDLLEGRYF SGALPDDEDV VGPGQESDDF ELSGSGDLDD LEDSMIGPEV VHPLVPLDNH IPERAGSGSQ VPTEPKKLEE NEVIPKRISP VEESEDVSNK VSMSSTVQGS NIFERTE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The specific activity is determined by binding ability in a functional ELISA. Immobilized recombinant human SYND4 at 500 ng/mL (100 μl/well) can bind recombinant human bFGF with a linear range of 0.1-10 ng/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. 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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Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. Human Syndecan-4 ECD shares approximately 79%, 78% and 81% aa identity with mouse, rat and porcine Syndecan-4 ECD, respectively. Syndecans are the best-characterized plasma membrane proteoglycans with two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. SYND4 is the most similar to SYND2, but is more universally expressed and is found in virtually every cell type. Expression can be upregulated by TGFβ2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator. SYND4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.   Product Properties   Synonyms Amphiglycan, MGC22217, Ryudocan, SDC4, syndecan 4, Syndecan4 Accession P31431 GeneID 6385 Source E.coli-derived human SYND4 protein,Glu19-Glu145. Molecular Weight Approximately 13.9 kDa. AA Sequence ESIRETEVID PQDLLEGRYF SGALPDDEDV VGPGQESDDF ELSGSGDLDD LEDSMIGPEV VHPLVPLDNH IPERAGSGSQ VPTEPKKLEE NEVIPKRISP VEESEDVSNK VSMSSTVQGS NIFERTE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The specific activity is determined by binding ability in a functional ELISA. Immobilized recombinant human SYND4 at 500 ng/mL (100 μl/well) can bind recombinant human bFGF with a linear range of 0.1-10 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by 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.   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.   Caution   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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CCL17, also known as thymus and activation-related chemokine (TARC), a small cytokine belonging to the C-C chemokine family. Among CC chemokine family members, CCL17 has approximately 24 - 29% amino acid sequence identity with RANTES, MIP-1 alpha, MIP-1 beta, MCP-1, MCP-2, MCP-3 and I-309. CCL17 is constitutively expressed in thymus, and at a lower level in lung, colon, and small intestine. CCL17 is also transiently expressed in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL17 has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL17 was identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells.   Product Properties Synonyms MGC138273, SCYA17, SCYA17MGC138271 Accession Q92583 GeneID 6361 Source E.coli-derived Human TARC/CCL17, Ala24-Ser93. Molecular Weight Approximately 8.1 kDa. AA Sequence ARGTNVGREC CLEYFKGAIP LRKLKTWYQT SEDCSRDAIV FVTVQGRAIC SDPNNKRVKN AVKYLQSLER S 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 T-lymphocytes 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, pH 7.4, 150 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 0.1-1.0mg/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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Transforming Growth Factor-alpha (TGF-α) , also known as sarcoma growth factor, TGF-type I and ETGF, is a member of the EGF family of cytokines. TGF-α is an EGF-related polypeptide growth factor that signals through the EGF receptor, and stimulates the proliferation of a wide range of epidermal and epithelial cells.Mature TGF-alpha shows approximately 93% amino acid sequence identity with mouse or rat TGF-alpha and is not species specific in its biological effects. Product Properties Synonyms Transforming Growth Factor alpha; TGF-a; TGF-type I; ETGF Accession P01135  Gene ID 7039 Source E.coli-derived Human TGF-a protein, Vla40-Ala89 Molecular Weight Approximately 5.8 kDa, on SDS-PAGE under reducing conditions AA Sequence V VSHFNDCPDS HTQFCFHGTC RFLVQEDKPA CVCHSGYVGA RCEHADLLA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity > 95% as determined by SDS-PAG Biological Activity Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 for this effect is < 0.4 ng/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method Formulation Lyophilized after extensive dialysis against PBS. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH₂O or PBS up to 100 μg/ml.For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. Avoid repeated freeze-thaw cycles.   Shipping and Storage The products are shipped with ice pack and can be stored at -80℃ for 1 year from date of receipt. 1week, 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. For your safety and health, please wear lab coats and disposable gloves for operation. 2. For research use only!

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TGFβ3 is a member of the TGF-β superfamily subgroup, defined by its structural and functional similarities. TGF-β3, along with β1 and β2, acts as a cellular switch to regulate immune function, cell proliferation, and epithelial-mesenchymal transition. The human TGF-β3 cDNA encodes a 412 amino acid (aa) precursor, which contains a 20 aa signal peptide and a 392 aa protein. Mature human TGF-β3 shares 100%, 99%, and 98% homology with mouse/dog/horse, rat, and pig TGF-β3, respectively. TGF-β3 has a high affinity for TGF-βRII, a type II serine/threonine kinase receptor. This receptor phosphorylates and activates the type I serine/threonine kinase receptor TGF-βRI or ALK-1 to regulate transcription through Smad phosphorylation. The product is provided in the form of a lyophilized (freeze-dried) powder, characterized by high activity, high purity, and low endotoxin levels. Product Properties Synonyms TGF-β3; ARVD; ARVD1; FLJ16571; LDS5; RNHF; TGFB3; TGFbeta 3; TGF-beta 3; TGF-beta3; TGF-beta-3; transforming growth factor beta-3; transforming growth factor beta 3 Uniprot No. P10600 Expression System and Range CHO-derived Human TGF-β3, Ala 301-Ser 412 Molecular Weight Approximately 13 kDa AA Sequence MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS Appearance White powder, Colorless clear liquid after reconstitution Purity ≥95%, by SDS-PAGE (under reducing (R) & Non-reducing conditions, visualized by Coomassie staining. Biological Activity Measured in a cell inhibition assay using TF-1 cells at IL4 presence. The ED50 for this effect is ≤0.2ng/mL. Endotoxin < 10 EU/mg of the protein by the LAL method Formulation Lyophilized from a 0.22 μm-filtered solution containing 100 mM Glycine, 150 mM NaCl, 5% mannitol and 0.01% Tween 80, pH 4.0   Method of Use It is recommended to centrifuge before opening the cap to bring the contents to the bottom, and then resuspend with sterile deionized water. Transportation and Storage Methods Store at -20°C, with a one-year shelf life upon receipt. After resuspension, store at 2~8°C for a shelf life of 7-10 days. After resuspension, store at -85 to -65°C for a shelf life of six months. It is recommended to aliquot and freeze for the first use to avoid repeated freeze-thaw cycles. Cautions 1.For your safety and health, please wear a lab coat and use disposable gloves when operating. 2.This product is intended for scientific research purposes only.

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TGF-beta 2 (transforming growth factor beta 2) is one of three closely related mammalian members of the large TGF-beta superfamily that share a characteristic cysteine knot structure. TGF-beta 1, -2 and -3 are highly pleiotropic cytokines proposed to act as cellular switches that regulate processes such as immune function, proliferation and epithelial-mesenchymal transition. Each TGF-beta isoform has some non-redundant functions; for TGF-beta 2, mice with targeted deletion show defects in development of cardiac, lung, craniofacial, limb, eye, ear and urogenital systems . Human TGF-beta 2 cDNA encodes a 414 amino acid (aa) precursor that contains a 19 aa signal peptide and a 395 aa proprotein. A furin-like convertase processes the proprotein to generate an N-terminal 232 aa latency-associated peptide (LAP) and a C-terminal 112 aa mature TGF- beta 2. Disulfide-linked homodimers of LAP and TGF-beta 2 remain non-covalently associated after secretion, forming the small latent TGF-beta 1 complex. Covalent linkage of LAP to one of three latent TGF-beta binding proteins (LTBPs) creates a large  latent complex that may interact with the extracellular matrix. Mature human TGF-beta 2 shows 100% aa identity with porcine, canine, equine and bovine TGF-beta 2, and 97% aa identity with mouse and rat TGF-beta 2. It demonstrates cross-species activity. Product Properties Synonyms Transforming Growth Factor beta 2 Accession P61812 Gene ID 7042 Source NS0-derived Human TGF-β2 protein, Ala303-Ser414 Molecular Weight Approximately 24 kDa AA Sequence ALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMIVKS CKCS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity > 97% as determined by SDS-PAGE. Biological Activity Measured by its ability to inhibit the IL-4-dependent proliferation of HT‑ 2 mouse T cells. The ED50 for this effect is 0.025-0.25 ng/mL. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method Formulation Lyophilized from 0.2 µm filtered concentrated solution in 35 % 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 4 mM HCl to a concentration of 0.1 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriately buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -70 °C 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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Thymic stromal lymphopoietin (TSLP) is an interleukin 7 (IL-7)-like cytokine originally characterized by its ability to promote the activation of B cells and dendritic cells (DCs). Both mouse TSLP and IL-7 can co-stimulate growth of thymocytes and mature T cells, and support B lymphopoiesis in long-term cultures of fetal liver cells and bone-marrow cells. Whereas mouse IL-7 facilitates the development of B220+/IgM- pre-B cells, mouse TSLP promotes the development B220+/IgM+ B cells. Human TSLP was reported   to preferentially stimulate myeloid cells; inducing the release of T cell-attracting chemokines from monocytes and enhancing the maturation of CD11c+ dendritic cells. Thymic stromal lymphopoietin (TSLP) is a cytokine expressed by epithelial cells, including keratinocytes, and is important in allergic inflammation. Subsequent studies have shown that TSLP promotes T helper type 2 (TH2) cell responses associated with immunity to some helminth parasites and the pathogenesis of many inflammatory diseases, including atopic dermatitis and asthma. TSLP can promote TH2 cytokine-associated inflammation by directly promoting the effector functions of CD4+ TH2 cells, basophils and other granulocyte populations while simultaneously limiting the expression of DC-derived proinflammatory cytokines and promoting regulatory T cell responses in peripheral tissues.   Product Properties Synonyms thymic stromal lymphopoietin Accession Q969D9 GeneID 85480 Source E.coli-derived Human TSLP, Tys29-Gln159, with an N-terminal Met Molecular Weight Approximately 15.1 kDa. AA Sequence MYDFTNCDFE KIKAAYLSTI SKDLITYMSG    TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ 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 IL-7Rα and human TSLP R co-transfected murine BaF3 pro-B cells is less than 0.3 ng/mL, corresponding to a specific activity of > 3.3× 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 20 mM PB, pH 7.4, 150 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 0.1-1.0mg/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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Thymosin Beta 4 is a naturally occurring peptide encoded by the TMSB4X gene located on Chr. X in humans. It is found in high concentrations in blood platelets, wound fluid and other tissues in the body. Tβ-4 is a major actin regulating peptide and the primary function is to stimulate the productions of T cells, which plays important part of the immune system. The thymosin beta-4 peptide, if used after a heart attack, might reactivate cardiac progenitor cells to repair damaged heart tissue.   Product Properties Synonyms Fx Accession P62328 GeneID 7114 Source E.coli-derived human Tβ-4 protein, Ser2-Ser44.  Molecular Weight Approximately 4.9 kDa. AA Sequence SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES 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 its ability to produce a protective effect against hydrogen peroxide in primary lung fibroblasts is in a concentration range of 0.5 - 10 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 20 mM PB, 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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TECK is a CC chemokine, specifically expressed by thymic stromal cells, and signals through the CCR9 receptor. TECK is chemotactic towards activated macrophages, thymocytes and dendritic cells. Recombinant Human TECK is a 14.3 kDa protein containing 127 amino acid residues, including the four conserved cysteine residues present in CC chemokines.   Product Properties Synonyms TECK, CCL25, SCYA25, Ckb15 Accession O15444 GeneID 6370 Source E.coli-derived Human CCL25 protein,Glu24-Leu150. Molecular Weight Approximately 14.3 kDa. AA Sequence MQGVFEDCCL AYHYPIGWAV LRRAWTYRIQ EVSGSCNLPA AIFYLPKRHR KVCGNPKSRE VQRAMKLLDA RNKVFAKLHH NTQTFQAGPH AVKKLSSGNS KLSSSKFSNP ISSSKRNVSL LISANSGL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% 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 monocytes is in a concentration range of 1.0-10 ng/ml. 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, pH 7.4, 150 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 0.1-1.0mg/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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TL-1A belongs to the TNF superfamily of ligands. It is expressed predominantly in endothelial cells, and to a lesser extent in the placenta, lung, kidney, skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis.   Product Properties Synonyms TL1A; TNF-like 1 Accession O95150 Source E.coli-derived Human TL-1A protein,Leu72-Leu251. Molecular Weight Approximately 20.5 kDa Purity > 97% by SDS-PAGE. 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, with 1% BSA. Reconstitution 1. We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile PBS, pH 7.4, with 0.1% BSA to a concentration of 0.1-1.0 mg/mL. 2. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. 3.Further dilutions should be made in PBS, which must contain carrier proteins, such as 0.1% BSA, 10% FBS, 5% HSA, 5% trehalose, one of four options.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year date of receipt. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ °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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Human TNF-alpha is a cytokine that plays a crucial role in the inflammatory response. It is produced by various immune cells such as macrophages and T-cells and is involved in the regulation of immune cell proliferation, differentiation, and apoptosis.   Product Properties Synonyms Tumor Necrosis Factor, TNFA, TNFSF2, Cachectin, Cytotoxin, Differentiation-inducing factor, DIF Uniprot No. P01375 Source E.coli-derived human TNF-α/TNFSF2 protein, Val77-Leu233, with C-terminal His tag. Molecular Weight Approximately 18.5 kDa. Purity > 95% as determined by SDS-PAGE. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with PBS. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution.   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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TWEAKR belongs to the TNF family of transmembrane proteins, and contains a cytoplasmic "death domain", which can activate a cell's apoptotic machinery. It is expressed in the spleen, thymus, peripheral blood lymphocytes, colon, and small intestine. Signal transduction by TWEAKR can be activated by either membrane-anchored or soluble TWEAK. Recombinant Human soluble TWEAKR is a 53 amino acid polypeptide (5.6 kDa) comprising the entire extracellular domain of the full-length TWEAKR protein.   Product Properties Synonyms TNFRSF12A, FGF-inducible 14, CD266 Accession Q9NP84  GeneID  51330 Source E.coli-derived Human TWEAK Receptor/TNFRSF12A protein,Glu28-Pro80. Molecular Weight Approximately 5.6 kDa Sequence EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP 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 inhibiting TWEAK-dependent proliferation of human umbilical vein endothelial cells (HUVEC) is less than 30ng/ml, corresponding to a specific activity of > 3.3 × 104 IU/mg, in the presence of 15 ng/mL of rHuTWEAK. 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 0.1-1.0mg/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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Thrombopoietin (TPO), is a key regulator of megakaryocytopoiesis and thrombopoiesis. The 353 amino acid (aa) human TPO precursor is cleaved to yield the 332 aa mature protein. Mature human TPO shares approximately 70% aa sequence homology with mouse and rat TPO. TPO and its receptor (c-Mpl) are the major regulators of megakaryocyte and platelet production and serve a critical and non-redundant role in hematopoietic stem cell (HSC) biology. TPO signals through the Jak-STAT, Ras-Raf-MAPK, and PI3K pathways, and promotes survival, proliferation, and polyploidization in megakaryocytes. The proto-oncogene c- also plays an important role in many of these same processes.   Product Properties Synonyms MGDF, MGDFC-mpl ligand, MKCSF, MK-CSF, ML, MPL ligand, MPLLG, THCYT1, THPO Accession NP_000451.1 Source HEK293 Cells-derived human TPO protein, Ser 22-Gly 353 with His tag at the N-terminus. Molecular Weight Approximately 37.6 kDa. As a result of glycosylation, TPO migrates as an approximately 78.2 kDa band in SDS-PAGE under reducing conditions. AA Sequence SPAPPACDL RVLSKLLRDS HVLHSRLSQC PEVHPLPTPV LLPAVDFSLG EWKTQMEETK AQDILGAVTL LLEGVMAARG QLGPTCLSSL LGQLSGQVRL LLGALQSLLG TQLPPQGRTT AHKDPNAIFL SFQHLLRGKV RFLMLVGGST LCVRRAPPTT AVPSRTSLVL TLNELPNRTS GLLETNFTAS ARTTGSGLLK WQQGFRAKIP GLLNQTSRSL DQIPGYLNRI HELLNGTRGL FPGPSRRTLG APDISSGTSD TGSLPPNLQP GYSPSPTHPP TGQYTLFPLP PTLPTPVVQL HPLLPDPSAP TPTPTSPLLN TSYTHSQNLS QEG Tag His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90 % by SDS-PAGE Biological Activity Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 for this effect is typically 10-60 ng/mL. 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 (400 μL) to a concentration of 0.25 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. 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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TACI, a member of the TNF Receptor superfamily, is expressed in the small intestine, spleen, thymus, peripheral blood leukocytes, activated T cells, and resting B cells. TACI can bind to both APRIL and BAFF, stimulate the activation of transcription factors NF-κB and AP-1, and can mediate the calcineurin-dependent activation of NF-AT (nuclear-factor of activated T cells). TACI also plays a key role in the stimulation of B and T cell function. Soluble TACI inhibits APRIL-stimulated proliferation of primary B cells by blocking the binding of APRIL to the membrane-anchored TACI receptor. Recombinant Human TACI is a soluble 159 amino acid polypeptide (17.8 kDa) comprising the TNFR homologous, cysteine-rich extracellular domain of the TACI protein.   Product Properties Synonyms TACI,TNFRSF13B Accession O14836 GeneID 23495 Source E.coli-derived Human Endostatin protein,Met1-Val160,with an N-terminal Met. Molecular Weight Approximately 18.0 kDa. AA Sequence MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV 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 biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/mL. 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 0.1-1.0mg/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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Trefoil factor 1 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides.  Mature human TFF1 shares 67% amino acid sequence identity with mouse and rat TFF1. The TFFs are stable secretory proteins expressed highly in the gastrointestinal tract (gastric mucosa). TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers. TFF1 inhibits the formation of calcium oxalate crystals, and its excretion in the urine is reduced in patients with kidney stones.   Product Properties Synonyms Breast Cancer Estrogen-inducible Protein, PNR-2, Polypeptide P1.A (hP1.A), Protein pS2 Accession P04155 GeneID 7031 Source E.coli-derived human TFF1 protein, Glu25-Phe84. Molecular Weight Approximately 13.2 kDa. AA Sequence EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF 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 chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 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, 150 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 0.1-1.0mg/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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Trefoil Factor 2 (TFF2), also known as spasmolytic peptide (SP), is one of three structurally related secreted proteins that contain trefoil domains. Trefoil factor 2 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. Mature human TFF2 shares 87% and 83% amino acid sequence identity with mouse and rat TFF2. The TFFs are stable secretory proteins expressed highly in the gastrointestinal tract (gastric mucosa). TFF2 can inhibit gastrointestinal motility and gastric acid secretion. Additionally, it functions as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains. Administration of TFF2 can reduce the severity of experimental colitis. TFF2 is down-regulated in many gastric cancers, although it is up-regulated in some breast cancers.   Product Properties Synonyms Spasmolysin, Spasmolytic polypeptide, SP Accession Q03403 GeneID 7032 Source E.coli-derived human TFF2 protein, Glu24-Tyr129. Molecular Weight Approximately 12.0 kDa. AA Sequence EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKS VEDCHY 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 chemotaxis bioassay using human MCF-7 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 20 mM PB, pH 7.4, 130 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 0.1-1.0mg/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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Trefoil Factor 3 (TFF3), also known as Intestinal Trefoil Factor (ITF) and P1.B, is one of three structurally related secreted proteins that contain trefoil domains. Trefoil factor 2 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. TFF-3 is expressed by goblet cells and in the uterus, and has also been shown to express in certain cancers, including colorectal, hepatocellular, and in biliary tumors. It involves in the maintenance and repair of the intestinal mucosa, also promotes the mobility of epithelial cells in healing processes. TFF3 up-regulation is associated with and enhances tumor cell invasion and metastasis. It supports hypoxia-induced VEGF up-regulation in tumor cells and also promotes angiogenesis in non-tumor environments. Over-expression of TFF3 in type 2 diabetic mouse liver has been shown to improve glucose tolerance and insulin sensitivity.   Product Properties Synonyms Intestinal Trefoil Factor, hITF, Polypeptide P1.B, hP1.B Accession Q07654 GeneID 7033 Source E.coli-derived human TFF3 protein, Glu36-Phe94. Molecular Weight Approximately 13.2 kDa. AA Sequence EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF 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 chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 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 0.1-1.0mg/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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  Name Catalog No. Size Recombinant Human TSHR Protein-VLP C230754E 20 μg C230754S 100 μg C230754M 100 μg C230754L 1 mg   Product Properties   Synonyms TSHR;LGR3 Source HEK293 Cells AA sequence Accession #P16473: Met1 - Leu764 Endotoxin < 1EU per μg by the LAL method. Purity > 85% as determined by DLS. Formulation 115mM Gly 4% trehalose Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage   The product should be stored at -85~-65℃ 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.        This product is for research use only.      

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TNF-β is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands, and signals through TNFR1 and TNFR2. TNF-β is produced by activated T and B lymphocytes, and has similar activities to TNF-α. Like TNF-α, TNF-β is involved in the regulation of various biological processes, including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-β forms heterotrimers with lymphotoxin-beta, which anchors TNF-β to the cell surface. TNF-β mediates the inflammatory, immunostimulatory, and antiviral response, involves in the formation of second lymphoid organs during development, has a role in apoptosis. TNF-β is produced by lymphocytes and cytotoxic for a variety of tumor cells in vitro.   Product Properties Synonyms TNFB, TNFSF1 Uniprot No. P01374 GeneID 4049 Source E.coli-derived Human Tumor Necrosis Factor-beta protein, Leu35-Leu205. Molecular Weight Approximately 18.7 kDa. AA Sequence LPGVGLTPSA AQTARQHPKM HLAHSTLKPA AHLIGDPSKQ NSLLWRANTD RAFLQDGFSL SNNSLLVPTS GIYFVYSQVV FSGKAYSPKA TSSPLYLAHE VQLFSSQYPF HVPLLSSQKM VYPGLQEPWL HSMYHGAAFQ LTQGDQLSTH TDGIPHLVLS PSTVFFGAFA L Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 5 pg/ml, corresponding to a specific activity of > 2.0 × 108 IU/mg in the presence of actinomycin D. 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 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 0.1-1.0mg/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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Uteroglobin, also called Clara cell secretory, phospholipid binding, 10 kDa or 16 kDa protein (CCSP, CCPBP, CC10 or CC16, respectively) is a small, non-glycosylated secreted protein of the secretoglobin superfamily, (designated 1A, member 1). Its name is derived from its very high expression in the pre-implantation uterus. It is produced by the non-ciliated, non-mucous secretory cells that predominate in lung bronchioles (Clara cells), and other non-ciliated epithelia that communicate with the external environment. Expression is induced by steroid hormones such as estrogen, and enhanced by the non-steroid hormone prolactin. Uteroglobin is found in blood, urine and other body fluids. Human Uteroglobin cDNA encodes a 21 amino acid (aa) signal sequence and a 70 aa mature protein. It shares 53 - 56% aa identity with mouse, rat, bovine, canine, equine or rabbit Uteroglobin, and is active in mice. The mature protein forms a disulfide-linked head-to-tail homodimer of 16 kDa. This homodimer is thought to form a binding pocket that binds hydrophobic ligands such as phospholipids, progesterone and retinols. Sequestering of prostaglandins and leukotrienes is anti-inflammatory, while sequestering of carcinogens such as polychlorinated bisphenols is anti-tumorigenic. Other immunoregulatory activities of Uteroglobin include cell migration inhibition (by binding the chemotaxis-related formyl peptide receptor FPR2 on dendritic cells), and the inhibition of T cell differentiation to a Th2 phenotype. A single nucleotide polymorphism of Uteroglobin, A38G, confers increased risk of asthma. Transglutaminase can crosslink Uteroglobin, either to itself or to other proteins such as the adhesion molecule fibronectin. Binding of fibronectin to Uteroglobin in the kidney is thought to protect against nephropathy, while binding of the lipocalin-1 receptor has been reported to suppress cancer cell motility and invasion.   Product Properties Synonyms CC10, CCSP, UGB Uniprot No. P11684 GeneID 7356 Source E.coli-derived Human Uteroglobin, Glu22-Asn91. Molecular Weight Approximately 15.8 kDa. AA Sequence EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% as determined by SDS-PAGE. Biological Activity The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0 μg/ml, corresponding to a specific activity of > 200 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, 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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CXCL17 also named dendritic cell and monocyte chemokine-like protein (DMC) and VEGF co-regulated chemokine 1 (VCC-1), is a small cytokine belonging to the CXC chemokine family. CXCL17 was the last chemokine ligand to be described and is the 17th member of the CXC chemokine family. Its strategic expression in mucosal tissues suggests that it is involved in innate immunity and/or sterility of the mucosa. Mature human DMC shares 73%, 71% and 64% amino acid sequence identity with bovine, mouse and rat DMC, respectively. It may be a housekeeping chemokine regulating recruitment of nonactivated blood monocytes and immature dendritic cells into tissues and may play a role in the innate defense against infections. CXCL17 also has a role in angiogenesis of importance for tumour develop   Product Properties Synonyms C-X-C Motif Chemokine 17, CXCL17, Dcip1, DMC, UNQ473, VCC-1, VEGF Coregulated Chemokine 1, VEGF Co-Regulated Chemokine 1 Accession Q6UXB2 GeneID 284340 Source E.coli-derived human VCC-1/CXCL17 protein, Ser22-Leu119. Molecular Weight Approximately 11.5 kDa. AA Sequence SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity than 5.0 μg/ml, corresponding to a specific activity of > 200 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 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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Vascular endothelial growth factor C (VEGF-C) and VEGF-D constitute a subfamily of the angiogenic VEGF angiogenic factors. VEGF-C is synthesized as a 58 kDa molecule that consists of a VEGF homolgy domain (VHD) flanked by N- and C-terminal propeptides. The proprotein undergoes covalent homodimerization and stepwise proteolytic processing to generate ligands with increasing affinity for VEGF R3/Flt-4. Fully processed VEGF-C containing just the 21 kDa VHD can additionally bind and activate VEGF R2/KDR/Flk-1. Fully processed human VEGF-C shares 98% amino acid sequence identity with mouse and rat VEGF-C. VEGF-C interactions with VEGF R3 are critical for lymphangiogenesis. VEGF-C and VEGF R3 are usually co-expressed at sites with lymphatic vessel sprouting, in the embryo, and in various pathological conditions. Over-expression of VEGF-C in tumor cells induces tumoral lymphatic hyperplasia, resulting in enhanced lymph flow and metastasis to regional lymph nodes. Product Properties Synonyms Flt4 ligand; Flt4-L; vascular endothelial growth factor C; Vascular endothelial growth factor-related protein; VEGFC; VEGF-C; VRPFLT4 ligand DHM Accession P49767 Source HEK293 Cells-derived human VEGF-C, Thr103-Arg227 with a C-terminal polyhistidine tag.  Molecular Weight The recombinant mature form of human VEGFC consists of 136 amino acids and has a predicted molecular mass of 15.5 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 22.5 kDa due to glycosylation. Tag His Purity > 95% by SDS-PAGE. Biological Activity 1. Measured by its binding ability in a functional ELISA. Immobilized VEGF C-his at2μg/mL(100 μL/well) can bind VEGFR3 hFc, the EC50 of VEGFR3 hFc is 2-15 ng/mL. 2. Scatchard analysis showed the affinity constant (Kd) of recombinant human VEGF-C bound to recombinant human VEGFR3 was 1.4 nM. 3. Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is typically 0.1-0.5 μg/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Concentration 0.95 mg/mL Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 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 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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Vascular endothelial growth factor D (VEGF-D), also known as c-fos-induced growth factor (FIGF), is a secreted glycoprotein of the VEGF/PDGF family. VEGFs regulate angiogenesis and lymphangiogenesis during development and tumor growth, and are  characterized by eight conserved cysteine residues that form a cystine knot structure. VEGF-C and VEGF-D, which share 23% amino acid (aa) sequence identity, are uniquely expressed as preproproteins that contain long N- and C-terminal propeptide extensions around the VEGF homology domain (VHD). Proteolytic processing of the 354 aa VEGF-D preproprotein creates a secreted proprotein. Further processing by extracellular serine proteases, such as plasmin or furin-like proprotein convertases, forms mature VEGF-D consisting of non- covalently linked 42 kDa homodimers of the 117 aa VHD. Mature human VEGF-D shares 94%, 95%, 99%, 97% and 93% aa identity with mouse, rat, equine, canine and bovine VEGF-D, respectively. It is expressed in adult lung, heart,  muscle, and small intestine, and is most abundantly expressed in fetal lungs and skin. Mouse and human VEGF-D are ligands for VEGF Receptor 3 (VEGF R3, also called Flt-4) that are active across species and show enhanced affinity when processed. Processed human VEGF-D is also a ligand for VEGF R2, also called Flk-1 or KDR. VEGF R3 is strongly expressed in lymphatic endothelial cells and is essential for regulation of the growth and differentiation of lymphatic endothelium. While VEGF-C is the critical ligand for VEGF R3 during embryonic lymphatic development, VEGF-D is most active in neonatal lymphatic maturation and bone growth. Both promote tumor lymphangiogenesis .  Product Properties Synonyms c-fos induced growth factor (vascular endothelial growth factor D); FIGF; vascular endothelial growth factor D; VEGFD; VEGF-D; VEGF-DVEGFDc-Fos-induced growth factor Accession O43915 Source HEK293 Cells-derived human VEGFD, Phe 93-Ser 201 with His tag at the C-terminu Molecular Weight The recombinant mature form of human VEGFD consists of 120 amino acids and has a predicted molecular mass of 13.6 kDa. In SDS-PAGE under reducing conditions, it migrates with an apparent molecular mass of 20-22 kDa due to glycosylation. Tag His Purity > 95% by SDS-PAGE. Biological Activity Measured in a cell proliferation assay using human umbilical vein endothelial cells (HUVEC). The ED50 for this effect is 0.3- 1.6 μg/mL Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Concentration 0.95 mg/mL 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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Vascular endothelial growth factor 121 (VEGF121) is a protein that plays a crucial role in the growth and survival of blood vessels. It stimulates the formation of new blood vessels, a process known as angiogenesis, which is essential for normal development and tissue repair. VEGF121 has therapeutic applications for conditions such as ischemic heart disease and cancer.   Product Properties Synonyms VEGFA; vascular permeability factor; vasculotropin;V EGF-A Uniprot No. P15692-9 Source Recombinant Human VEGF121 Protein is expressed from HEK293 Cells with His tag at the C-terminal. It contains Ala27-Arg147. Molecular Weight The protein has a predicted MW of 16 kDa. And it migrates as 17-25 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greater than 100 ug/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 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. 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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