Products

CNTF protein is a neurotrophic factor that promotes neuronal survival and differentiation. It is involved in the regulation of various cellular processes, such as inflammation, metabolism, and immune response. CNTF has potential therapeutic applications for the treatment of neurodegenerative diseases.   Product Properties   Synonyms HCNTF,ciliary neurotrophic factor Source Recombinant Human CNTF Protein is expressed from HEK293 Cells with His tag at the N-terminal. It contains Met1-Met200. Endotoxin < 0.01 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Human Complement 5a (C5a) is an enzymatically generated glycoprotein that belongs to a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 74 amino acid (aa) peptide that is created by the activity of C5a convertase on the C5 alpha -chain. Human C5a has four alpha -helices plus three intrachain disulfide bonds that create a triple loop structure. In serum, proteolytic processing removes the Cterminal arginine, creating a low activity C5adesArg74 molecule. Human C5a is 60% and 54% aa identical to mouse and rat C5a, respectively. C5a binds to a signaling G-protein coupled receptor (C5aR/CD88) and a nonsignaling GPCR termed C5L2. Activation of Cd88 results in neutrophil chemotaxis and endothelial cell activation. It also triggers an oxidative burst in macrophages and neutrophils, and induces release of histamine in basophils and mast cells. Product Properties Synonyms CPAMD4 Accession P01031 GeneID 727 Source E.coli-derived Human C5a, Thr678-Arg751. Molecular Weight Approximately 8.3 kDa. AA Sequence TLQKKIEEIA AKYKHSVVKK CCYDGACVNN DETCEQRAAR ISLGPRCIKA FTECCVVASQ LRANISHKDM QLGR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml. Fully biologically active when compared to standard.  Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions. Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ 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 Avoid repeated freeze-thaw cycles. For your safety and health, please wear lab coats and disposable gloves for operation. For research use only!

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CCL27, also known as CTACK (cutaneous T cell-attracting chemokine), ALP, ILC, and ESkine, is a member of the CC family of chemokines. Mature human CCL27 is an 88 amino acid (aa) protein that shares 57% aa sequence identity with mouse and rat CCL27. It shares 11% - 35% aa sequence identity with other human CC chemokines. An alternately spliced form of mouse CCL27, known as PESKY, is localized to the nucleus and promotes cellular migration. CCL27 is constitutively expressed by keratinocytes and is upregulated by inflammatory stimuli and in wounded skin. CCL27 binds the chemokine receptor CCR10, glycosaminoglycans in the extracellular matrix, sulfated tyrosine residues on PSGL-1, and determinants on the surface of fibroblasts and endothelial cells . CCL27 cooperates with CCL17/TARC in inducing the migration of cutaneous lymphocyte antigen (CLA) positive memory T cells to  the skin during inflammation. Endothelial cell-bound CCL27 can mediate the adhesion of those cells to CLA+ T cells. CCL27 also induces the migration of keratinocyte precursors from bone marrow to the skin, thereby promoting wound healing. In humans, serum CCL27 levels are elevated and correlate with disease severity in atopic dermatitis, psoriasis vulgaris, and mycosis fungoides.   Product Properties   Synonyms CTACK Source E.coli-derived Human B cell Activating Factor Rececptor protein,Phe25-Gly112. AA Sequence FLLPPSTACC TQLYRKPLSD KLLRKVIQVE LQEADGDCHL QAFVLHLAQR SICIHPQNPS LSQWFEHQER KLHGTLPKLN FGMLRKMG Endotoxin < 0.1 EU per μg by the LAL method. Purity > 96% by SDS-PAGE and HPLC analyses. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL.   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. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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CXCL12, also known as SDF-1, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC 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. They are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. CXCL12 binds primarily to CXC receptor 4. The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. CXCL12 also can influence lymphopoiesis and regulate patterning and cell number of neural progenitor.   Product Properties   Synonyms SDF-1 alpha, hSDF-1 alpha, IRH, hIRH, PBSF Accession P48061 GeneID 6387 Source E.coli-derived Human SDF-1α/CXCL12α, Lys22-Lys89 Molecular Weight Approximately 8.0 kDa. AA Sequence KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK 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 20 mM PB pH 7.0, 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 0.1-1.0 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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CXC chemokine ligand 16 (CXCL16) is a type I membrane protein containing a non-ELR motif-containing CXC chemokine domain in its extracellular region. Functional CXCL16 can be shed from the cell surface as an approximately 35 kDa soluble protein.   Product Properties Synonyms   CXCLG16, SR-PSOX，SRPSOX   Uniprot No.  Q9H2A7-1 Source Recombinant Human CXCL16 Protein is expressed from E.coli Cells with tag free. It contains Asn 30 - Thr 205. Molecular Weight The protein has a predicted MW of 19.5kDa. Purity > 95% as determined by SDS-PAGE. Endotoxin <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. The concentration of protein solution used for lyophilization is generally 1mg/mL. Dissolve lyophilized protein with sterile water 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.Please operate with lab coats and disposable gloves,for your safety.

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  Name Catalog No. Size Recombinant Human CXCR1 Protein-VLP C230741E 20 μg C230741S 100 μg C230741M 100 μg C230741L 1 mg   Product Properties   Synonyms CXCR1 / CMKAR1 / IL8RA Source HEK293 Cells AA sequence Accession #P25024:Met1 - Leu350 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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  Name Catalog No. Size Recombinant Human CXCR4 Protein-VLP C230742E 20 μg C230742S 100 μg C230742M 100 μg C230742L 1 mg   Product Properties   Synonyms CD184,Fusin,D2S201E,FB22,HM89,HSY3RR,LAP3,LCR1,LESTR,NPY3R Source HEK293 Cells AA sequence Accession #P61073:Met1 - Ser352 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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The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.   Product Properties Synonyms PPIF, Cyclophilin F, CyP-M, Rotamase F Accession P30405 GeneID 10105 Source E.coli-derived Human CyP-D, Cys30-Ser207. Molecular Weight Approximately 18.9 kDa. AA Sequence CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS Tag None Physical Appearance Sterile colorless liquid. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Supplied as a 0.2 μm filtered solution in PBS, pH7.4, with 1 mM DTT, 10 % glycerol.   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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Cyr61, also known as CCN1,is a 40-45 kDa matricellular glycoprotein that plays an important role in cellular adhesion and migration. Cyr61 consists of an IGFBP domain, a VWF type C domain, a TSP type I domain, and a cysteine knot domain. Mature human Cyr61 shares 93% amino acid sequence identity with mouse and rat Cyr61. It is widely expressed during development and in adult tissues  (2, 3). Cyr61 associates with the extracellular matrix (ECM) and with many cell surface molecules including Integrins alpha V beta 3, alpha V beta 5, alpha M beta 2, and alpha 6 beta 1, Syndecan-4, and heparan sulfate proteoglycans. Cyr61 mediates the adhesion and migration of multiple cell types and also promotes vascular endothelial cell tubule formation. Plasmin  cleavage  of ECM-bound Cyr61 releases a 28 kDa N-terminal fragment which retains the ability to promote endothelial cell migration. Cyr61 exhibits both tumorigenic and tumor suppressor properties.   Product Properties Synonyms CCN1, Cysteine-rich Angiogenic Inducer 61, GIG1, IGFBP-10 Accession O00622 GeneID 3491 Source E.coli-derived Human CYR61 protein,Thr25-Asp381. Molecular Weight Approximately 39.4 kDa AA Sequence TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD 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 a cell proliferation assay using murine Balb/3T3 cells is less than 3.0 μg/mL, corresponding to a specific activity of > 330 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method Formulation Lyophilized from a 0.2μm 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℃ 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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Recombinant Human Cystine/glutamate transporter (SLC7A11) (Active)    Name Catalog No. Size Recombinant Human Cystine/glutamate transporter (SLC7A11) C230783E 20 μg C230783S 100 μg C230783M 100 μg C230783L 1 mg   Product Properties Synonyms (Amino acid transport system xc-)(Calcium channel blocker resistance protein CCBR1)(Solute carrier family 7 member 11)(xCT) Source In vitro E.coli expression system AA sequence Accession # Q9UPY5, Met1 -  Leu501 MW 58.2KD Tag N-terminal 10xHis-tagged Purity >90% as determined by SDS-PAGE. Formulation Liquid: Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder:  Tris/PBS-based buffer, 6% Trehalose. Activity ELISA: Immobilized Human SLC7A11 at 2 μg/mL can bind Anti-SLC7A11 recombinant antibody, the EC50 is 9.452-13.79 ng/mL. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Please reconstitute protein in deionized sterile water or PBS to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference. Figure MW and purity analysis by discontinuous SDS-PAGE (reduced). ELISA analysis of its binding ability. Immobilized Human SLC7A11 at 2μg/mL can bind Anti-SLC7A11 recombinant antibody, the EC50 is 9.452-13.79 ng/mL. Loaded Anti-Human SLC7A11 Antibody on 96-Flat plate, can bind Human SLC7A11, with an affinity constant of ＜1 pM as determined in BLI assay (Gator Prime). Storage Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. Cautions Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

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Desert Hedgehog (Dhh) belongs to the highly conserved Hedgehog family of proteins which are involved in multiple developmental processes. Desert Hedgehog is a secreted, 45 kDa, 373 amino acid (aa) protein that undergoes autocatalytic cleavage between Gly198 and Cys199 catalyzed by the C-terminal domain, which releases the N-terminal domain with a concominant attachment of cholesterol at its new C-terminus. In addition to the C-terminally attached cholesterol, a fatty acid acyl chain is esterified to the N-terminal cysteine (aa 23) via an amide linkage. The 19 kDa N-terminal signaling domain is membrane associated due to its double lipid modifications. Its binding to Patched receptors results in the loss of Patched repression of Smoothened signaling. Dhh binds both Patched and Patched 2 as well as Hedgehog interacting protein (Hip). Within the N-terminal domain, human Dhh shares 97% aa sequence identity with mouse and rat Dhh. It shares approximately 75% aa seqeuence identity with human Indian (Ihh) and Sonic Hedgehog (Shh). Dhh is produced by Sertoli cells and is required for testis development and spermatogenesis. It induces steroidogenic factor 1, which is instrumental in promoting Leydig cell differentiation. It also promotes the deposition of basal lamina surrounding seminiferous tubules. Mutations of Dhh are linked to complete pure gonadal dysgenesis. Dhh is expressed in the female by ovarian granulosa cells and the corporus luteum. Its upregulation in ovarian cancer correlates positively with proliferative index, and negatively with prognosis. Dhh is also expressed by Schwann cells and is upregulated following nerve injury. It induces the expression of Patched and Hip in neural tissue fibroblasts and promotes the formation of the connective tissue sheath surrounding peripheral nerves.   Product Properties Synonyms DHH; HHG-3MGC35145 Accession O43323 GeneID 50846 Source E.coli-derived Human DHH C23II, Cys23-Gly198. Molecular Weight Approximately 19.9 kDa. AA Sequence IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to induce alkaline phosphatase production by C3H10T1/2(CCL-226) cells is 15-45 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 10mM PB, pH 6.0, 300mM 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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Dickkopf related protein 1 (Dkk-1) is the founding member of the Dickkopf family of proteins that includes Dkk-1, -2, -3, -4, and a related protein, Soggy. Dkk proteins are secreted proteins that contain two conserved cysteine-rich domains separated by a linker region. Each domain contains ten cysteine residues . Mature human Dkk-1 is a 40 kDa glycosylated protein that shares 86%, 87%, 90% and 91% aa sequence identity with mouse, rat, rabbit and bovine Dkk-1, respectively. It also shares 42% and 36% aa identity with human Dkk-2 and Dkk-4, respectively. Dkk-1 and Dkk-4 are well documented antagonists of the canonical Wnt signaling pathway. This pathway is activated by Wnt engagement of a receptor complex composed of the Frizzled proteins and one of two low-density lipoprotein receptor-related proteins, LRP5 or LRP6 . Dkk-1 antagonizes Wnt by forming ternary complexes of LRP5/6 with Kremen1 or Kremen2. Dkk- 1/LRP6/Krm2 complex internalization has been shown to down-regulate Wnt signaling. Dkk-1 is expressed throughout development and antagonizes Wnt-7a during limb development. Other sites of expression include developing neurons, hair follicles and the retina of the eye .   Product Properties Synonyms Dickkopf-1;DKK-1;SK Protein; DKK1; dkk1; dkk-1 Accession O94907 Source HEK293 Cells-derived human Dkk-1 protein, Met2-His 266 with His tag at the C-terminus. Molecular Weight Approximately 27.2 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh DKK1 is approximately 42.9 kDa due to glycosylation. AA Sequence MALGAAGAT RVFVAMVAAA LGGHPLLGVS ATLNSVLNSN AIKNLPPPLG GAAGHPGSAV SAAPGILYPG GNKYQTIDNY QPYPCAEDEE CGTDEYCASP TRGGDAGVQI CLACRKRRKR CMRHAMCCPG NYCKNGICVS SDQNHFRGEI EETITESFGN DHSTLDGYSR RTTLSSKMYH TKGQEGSVCL RSSDCASGLC CARHFWSKIC KPVLKEGQVC TKHRRKGSHG LEIFQRCYCG EGLSCRIQKD HHQASNSSRL HTCQRH Tag His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90% by SDS-PAGE. Biological Activity Measured by its ability to inhibit Wnt3a-induced alkaline phosphatase production by C3H10T1/2 cells. The ED50 for this effect is approximately 0.1-0.4 μg/mL in the presence of 10 ng/mL of mouse Wnt3a. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Epidermal Growth Factor (EGF) is a small growth factor containing 53 amino acid residues capable of stimulating the proliferation of both mesenchymal and epithelial cells. The mature protein is much smaller, only 53 aa, and is generated by proteolytic cleavage of the EGF domain proximal to the transmembrane region. EGF is well conserved across mammals with mature human EGF 70% identical to mature mouse and rat EGF. EGF and fibroblast growth factor 2 (FGF-2) induce the proliferation of neural precursor cells isolated from specific regions of the embryonic and adult brain. EGF and somatomedin C-supplemented medium was shown to be capable of replacing the progression activity of 5% platelet-poor  plasma  (PPP)  for  competent  density-inhibited  BALB/c-3T3 cells. Biological activities ascribed to EGF include epithelial development, angiogenesis, inhibition of gastric acid secretion, fibroblast proliferation, and colony formation of epidermal cells in culture.   Product Properties Synonyms Urogastrone, URG Accession P01133 GeneID 1950 Source E.coli-derived Human EGF, Asn971-Arg1023. Molecular Weight Approximately 6.2 kDa. AA Sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared 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 ℃ 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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Human epidermal growth factor (EGF) protein is a naturally occurring protein that plays a vital role in cell growth and development. It is produced and released by various cells in the body, including the skin, salivary glands, and kidneys. human EGF protein is a vital protein in the body that plays a crucial role in cell growth, tissue regeneration, and overall health. Its inclusion in various skincare products has made it a popular ingredient in the pursuit of healthier and more youthful-looking skin.   Product Properties Synonyms EGF, URG, HOMG4 Uniprot No. P01133 Source Human EGF Protein is expressed from E.coli with no tag . It contains Asn971-Arg1021.  AA Sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E Molecular Weight Approximately 6.0 kDa. Purity > 98% as determined by SDS-PAGE. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. 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 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.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The human EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Human EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.   Product Properties Synonyms Endocrine Gland-derived Vascular Endothelial Growth Factor, Prokineticin 1, PROK1 Accession P58294 GeneID 84432 Source E.coli-derived Human EG-VEGF protein,Ala20-Phe105. Molecular Weight Approximately 9.7 kDa. AA Sequence AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using bovine EJG cells is less than 2.0 μg/mL, corresponding to a specific activity of > 500 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, 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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Endostatin is a naturally-occurring 20-kDa C-terminal fragment derived from collagen alpha-1(XVIII) chain (COL18A1). It is reported to serve as an anti-angiogenic agent, similar to angiostatin and thrombospondin. It potently inhibits endothelial cell proliferation and inhibits endothelial cell angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling. Endostatin is a broad spectrum angiogenesis inhibitor and may interfere with the pro-angiogenic action of growth factors such as basic fibroblast growth factor (bFGF/FGF-2) and vascular endothelial growth factor (VEGF).   Product Properties Synonyms Human Endostatin Accession P39060 GeneID 80781 Source E.coli-derived Human Endostatin protein,His1572-Lys1754. Molecular Weight Approximately 20.1 kDa. AA Sequence HSHRDFQPVL HLVALNSPLS GGMRGIRGAD FQCFQQARAV GLAGTFRAFL SSRLQDLYSI VRRADRAAVP IVNLKDELLF PSWEALFSGS EGPLKPGARI FSFDGKDVLR HPTWPQKSVW HGSDPNGRRL TESYCETWRT EAPSATGQAS SLLGGRLLGQ SAASCHHAYI VLCIENSFMT ASK 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 ED50 as determined by inhibiting the FGF basic-dependent proliferation of HUVEC migration is less than 2.0 µg/mL in the presence of Anti-Human Endostatin Polyclonal Antibody. 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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Eotaxin-2 is a CC chemokine that signals through the CCR3 receptor. It is produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3, including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Additionally, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which also includes a C-terminal truncation, contains 78 amino acid residues (92 amino acid residues for the murine homolog, without C-terminal truncation). Eotaxin-2 contains the four conserved cysteine residues present in CC chemokines. Recombinant Human Eotaxin-2 is an 8.8 kDa protein containing 78 amino acid residues.   Product Properties Synonyms CK-beta-6, MPIF-2, Small-inducible Cytokine A24 Accession O00175 GeneID 6369 Source E.coli-derived Human CCL24 protein,Vla27-Ala104. Molecular Weight Approximately 8.8 kDa AA Sequence VVIPSPCCMF FVSKRIPENR VVSYQLSSRS TCLKAGVIFT TKKGQQFCGD PKQEWVQRYM KNLDAKQKKA SPRARAVA 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 peripheral blood eosinophils is in a concentration of 50-100 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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Eotaxin-3, also named CCL26 or SCYA26, is a novel human CC chemokine. The eotaxin subfamily of CC chemokines consists of eotaxin-1/CCL11, eotaxin-2/CCL24 and eotaxin-3/CCL26. Eotaxin-3/CCL26 has been shown to be expressed by several different  cell types, including basophils, dendritic cells, smooth muscle cells, epithelial cells and fibroblasts. Interleukin (IL)-4 is the main inducer for eotaxin-3 expression, whereas eotaxin-1 is up-regulated by IL-4 and the proinflammatory cytokine tumour necrosis factor (TNF)-α. Eotaxin-3 is expressed in vascular endothelial cells and human dermal fibroblasts after IL-4 and IL-13 stimulation, and this is dependent upon the IL-4-/IL-13-specific transcription factor, signal transducers and activator of transcription (STAT)-6. Eotaxin-3 is expressed on the surface of IL-4-stimulated endothelial cells and promotes eosinophil transmigration. Eotaxin-3/CCL26 induces calcium flux in eosinophils as well as in CCR3-transfected cells. Eotaxin-3/CCL26 has also been shown to cross-desensitize cells to other CCR3 ligands.   Product Properties Synonyms CC chemokine IMAC, MIP-4-alpha, TSC-1 Accession Q9Y258 GeneID 10344 Source E.coli-derived Human Eotaxin-3/CCL26, Thr24-Leu94. Molecular Weight Approximately 8.4 kDa. AA Sequence TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L 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 CCR3 transfected HEK293 cells is in a concentration range of 0.5-2.0 μg/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. 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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Human CCL11 is belonging to the CC chemokine family. It is encoded by the gene CCL11. CCL11 was first purified from bronchoalveolar lavage fluid of guinea pigs. It was a strong and specific eosinophil chemoattractant in vitro. It can directly chemotactic for eosinophils, but not for monocytes or neutrophils. Human CCL11 is approximately 63 % identical at the amino acid level to murine CCL11. In addition, CCL11 also shows about 60 % amino acid sequence identity to human MCPs. CCR3 has been identified to be a specific CCL11 receptor.   Product Properties Synonyms SCYA11 Protein, Human; Small-inducible cytokine A11 Accession P51671 GeneID 6356 Source E.coli-derived human Eotaxin Protein, Gly24-Pro97 Molecular Weight Approximately 8.4 kDa. AA Sequence GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDIC ADPKKKWVQD SMKYLDQKSP TPKP 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 peripheral blood eosinophils is in a concentration range of 0.1-10.0 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 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Epididymis Protein 4, also known as Epididymal secretory protein E4, Major epididymis-specific protein E4, Putative protease inhibitor WAP5, WFDC2 and HE4, is a secreted protein that contains two WAP domains. WFDC2 / HE4 is a member of a family of stable 4-disulfide core proteins that are secreted at high levels. It is expressed in a number of normal tissues, including male reproductive system, regions of the respiratory tract and nasopharynx. It is highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines. Initially described as being exclusively transcribed in the epididymis. WFDC2 may be a component of the innate immune defences of the lung, nasal and oral cavities and suggest that WFDC2 functions in concert with related WAP domain containing proteins in epithelial host defence. WFDC2 re-expression in lung carcinomas may prove to be associated with tumour type and should be studied in further detail. Mammary gland expression of tammar WFDC2 during the course of lactation showed WFDC2 was elevated during pregnancy, reduced in early lactation and absent in mid-late lactation. WFDC2 / HE4 can undergo a complex series of alternative splicing events that can potentially yield five distinct WAP domain containing protein isoforms.   Product Properties Synonyms HE4; WAP5 Uniprot No. Q14508 Gene ID 10406 Source E.coli-derived Human E4, Glu31-Phe124.  AA Sequence EKTGVCPELQ ADQNCTQECV SDSECADNLK CCSAGCATFC SLPNDKEGSC PQVNINFPQL GLCRDQCQVD SQCPGQMKCC RNGCGKVSCV TPNF Molecular Weight Approximately 10.0 kDa. Purity > 95% by SDS-PAGE. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.0. Application WB, ELISA   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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Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, and heart, as well as in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant Human Epigen is a 7.9 kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF-homologous portion of the Epigen precursor.   Product Properties Synonyms EPG, Epithelial Mitogen Accession Q6UW88 GeneID 255324 Source E.coli-derived Human Epigen protein,Ala24-Ala104. Molecular Weight Approximately 7.9 kDa. AA Sequence AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity using murine Balb/c 3T3 cells is less than 300 ng/mL, corresponding to a specific activity of > 3.3 × 10 3 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Epiregulin is an EGF-related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes, as well as in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant Human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.   Product Properties Synonyms EREG Accession O1494 GeneID 2069 Source E.coli-derived Human Epiregulin protein,Val60-Leu108 Molecular Weight Approximately 5.6 kDa. AA Sequence AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA 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 a cell proliferation assay using murine Balb/c 3T3 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 10 5 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2μm 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℃ 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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CXCL5, also known as epithelial cell-derived neutrophil-activating peptide (ENA-78), is an 8 kDa proinflammatory member of the CXC chemokine family. Its Glu-Leu-Arg (ELR) motif confers angiogenic properties and distinguishes it from ELR-CXC chemokines which are angiostatic. CXCL5 is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. It also can be detected in eosinophils, and can be inhibited with the type II interferon. In vivo, CXCL5 is elevated at sites of inflammation and pulmonary fibrosis where it promotes neutrophil infiltration and activation as well as angiogenesis. Its up-regulation contributes to increased vascularization, tumor growth, and metastasis in many cancers. CXCL5 plays a role in reducing sensitivity to sunburn pain in some subjects, and is a potential target which can be utilized to understand more about pain in other inflammatory conditions like arthritis and cystitis. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2.   Product Properties Synonyms ENA-78 (5-78), CXCL5 (5-78), Neutrophil Activating Peptide ENA-78, Small-inducible cytokine B5 Accession P42830 GeneID 6374 Source E.coli-derived Human ENA-78, 5-78 aa/CXCL5, Ala41-Asn114. Molecular Weight Approximately 8.1 kDa. AA Sequence AAVLRELRCV CLQTTQGVHP KMISNLQVFA IGPQCSKVEV VASLKNGKEI CLDPEAPFLK KVIQKILDGG NKE 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 peripheral blood neutrophils is in a concentration of 10.0-100.0 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, 50 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Erythropoietin (EPO) is a 34 kDa glycoprotein hormone in the type I cytokine family and is related to thrombopoietin. Its three N-glycosylation sites, four alpha helices, and N- to C-terminal disulfide bond are conserved across species. Glycosylation of the EPO protein is required for biological activities in vivo . The mature human EPO protein shares 75% - 84% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat EPO. EPO is primarily produced in the kidney by a population of fibroblast-like cortical interstitial cells adjacent to the proximal tubules. It is also produced in much lower, but functionally significant amounts by fetal hepatocytes and in adult liver and brain. EPO promotes erythrocyte formation by preventing the apoptosis of early erythroid precursors which express the erythropoietin receptor (EPO R). EPO R has also been described in brain, retina, heart, skeletal muscle, kidney, endothelial cells, and a variety of tumor cells . Ligand induced dimerization of EPO R triggers JAK2-mediated signaling pathways followed by receptor/ligand endocytosis and degradation. Rapid regulation of circulating EPO allows tight control of erythrocyte production and hemoglobin concentrations.   Product Properties Synonyms Erythropoietin, Epoeti Accession P01588 GeneID 2056 Source HEK293 Cells-derived human EPO protein, Met1-Arg193 with hFc Tag at the C-terminu Molecular Weight Approximately 45.1 kDa. AA Sequence MGVHECPAWL WLLLSLLSLP LGLPVLGAPP RLICDSRVLE RYLLEAKEAE NITTGCAEHC SLNENITVPDTKVNFYAWKR MEVGQQAVEV WQGLALLSEA VLRGQALLVN SSQPWEPLQL HVDKAVSGLR SLTTLLRALG AQKEAISPPD AASAAPLRTI TADTFRKLFR VYSNFLRGKL KLYTGEACRT GDR Tag hFc Tag Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.  Purity > 95% by SDS-PAGE. Biological Activity 1. Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is 2.0-8.0 ng/mL. 2. Measured by its ability to bind Human EPOR (ECD, His Tag) in functional ELISA. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ 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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CCL21, also known as 6Ckine, TCA-4, SLC, Exodus-2, and A21, is a 12 kDa homeostatic chemokine. Some of the chemokines are considered pro-inflammatory which can be induced to recruit cells of the immune system to a site of infection during an immune response, while others are considered homeostatic and are implied in controlling the migration of cells during normal processes of tissue maintenance and development. CCL21 takes its name 6Ckine for its consititutively six conserved cysteine residues but not four cysteines typical to chemokines. CCL21 has function in ininducing vigorous calcium migrations and chemotactic responses. During chronic inflammation or tissue damage, CCL21 is up-regulated on local vascular endothelial cells, macrophages, T cells, and neurons. In these settings, it promotes fibrosis, inflammatory cytokine production, and neuropathic pain. The soluble chemokine is elevated in rheumatoid arthritis synovial fluid and in the serum of coronary artery disease patients. CCL21 has been shown to exert either angiogenic or angiostatic effects. These effects, in combination with the ability of CCL21 to attract immune suppressor cells (Treg and MDSC) to a tumor site can have positive or negative effects on tumor progression.   Product Properties Synonyms 6Ckine, Beta-chemokine Exodus-2, SLC Accession O00585 GeneID 6366 Source E.coli-derived Human Exodus-2/CCL21, Ser24-Pro134. Molecular Weight Approximately 12.2 kDa. AA Sequence SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCK RTERSQTPKG P 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 lymphocytes is in a concentration range of 10-100 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 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℃. 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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Fatty acid binding protein-3 (FABP3; also named Fatty acid binding protein 11, FABP11, H- or M- (heart or muscle) FABP, Mammary derived growth inhibitor, or MDGI) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner. FABP3 is one of ten cytoplasmic FABPs that are 14-15 kDa in size and range from 126-140 amino acids (aa) in length. Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. The FABP family members are subdivided based on organ or tissue type it was originally expressed or identified; liver- (L-FABP), intestine- (I-FABP), heart- (H-FABP), adipocyte- (A-FABP), epidermal- (E-FABP), ileal- (IL-FABP), brain- (B-FABP), myelin- (M-FABP) and testis-FABP (T-FABP). Human H-FABP, the product of the FABP3 gene, is a 132 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha - helices. One molecule of FABP3 is capable of binding one long-chain fatty acid. It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand. Human FABP3 is 86%, 89% and 89% aa identical to mouse, rat and canine FABP3, respectively. It also shows 29% and 32% aa identity to human L-FABP and I- FABP, respectively.   Product Properties Synonyms FABP11;HFABP;MDGI Accession P05413 GeneID 2170 Source E.coli-derived Human FABP3, Val2-Ala133. Molecular Weight Approximately 14.7 kDa. AA Sequence VDAFLGTWKL VDSKNFDDYM KSLGVGFATR QVASMTKPTT IIEKNGDILT LKTHSTFKNT EISFKLGVEF DETTADDRKV KSIVTLDGGK LVHLQKWDGQ ETTLVRELID GKLILTLTHG TAVCTRTYEK EA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE. Biological Activity Testing in progress. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 10mM PB,150 mM NaCl,1 mM DTT, 0.1 % tween-20, 5 % trehalose, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fatty acid binding protein-2 (FABP-2; also named I- or intestinal FABP) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner. FABP-2 is one of nine cytoplasmic FABPs that are 14-15 kDa in size and range from 126-134 amino acids (aa) in length. Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. Nevertheless, based on aa sequence, the nine FABP family members have been shown to form three subgroups, with FABP- 2/I- FABP linked with liver/L-FABP and heart/H-FABP. The designation of a tissue type, such as intestinal, does not suggest the binding protein is universally expressed in all cell types that make up the organ or tissue. Human I-FABP, the product of the FABP-2 gene, is a 132 aa cytosolic protein that shows a flattened beta -barrel structure (called a beta -clam) generated by a series of antiparallel beta -strands and two alpha - helices. Preferred ligands for FABP-2 include sixteen to twenty carbon long chain fatty acids. It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand. An Ala-to-Thr polymorphism at position #54 has been reported to potentially impact FABP-2 function. This polymorphism has been suggested to be associated with an increased risk of type II diabetes. To date, the evidence appears to be equivocal. This polymorphism may, however, have unusual metabolic effects depending upon the type of diet involved. Human FABP-2 is 78%, 82% and 86% aa identical to mouse, rat and canine FABP-2, respectively. It also shows 33% and 24% aa identity to human H-FABP and L- FABP, respectively. FABP-2 is proposed to transport fatty acids (FA) into cells, increase FA availability to enzymes, protect cell structures from FA attack, and target FA to transcription factors in the nuclear lumen.   Product Properties Synonyms IFABP; I-FABP Accession P12104 GeneID 2169 Source E.coli-derived Human FABP2, Ala2-Asp132. Molecular Weight Approximately 15.1 kDa. AA Sequence AFDSTWKVDR SENYDKFMEK MGVNIVKRKL AAHDNLKLTI TQEGNKFTVK ESSAFRNIEV VFELGVTFNY NLADGTELRG TWSLEGNKLI GKFKRTDNGN ELNTVREIIG DELVQTYVYE GVEAKRIFKK D Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin < 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 7.0 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℃. 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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Fatty acid binding protein-6 (FABP6), also known as ileal bile acid binding protein (I-BABP) and gastrotropin, is a 15 kDa cytoplasmic protein that belongs to the FABP family. It is expressed in ileal epithelium and multiple other tissues. Alternate transcription promoters generate two transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is believed to be acetylated on Ala2. It binds both fatty acids and bile acids and has roles in fatty acid transport and metabolism. The amino acid sequence of human FABP6 is 80%, 78%, and 75% aa identical to that of mouse, canine, and porcine FABP6, respectively.   Product Properties Synonyms I-BALB; I-BAP Accession P51161 GeneID 2172 Source E.coli-derived Human FABP6, Val2-Ala133 Molecular Weight Approximately 14.7 kDa AA Sequence VDAFLGTWKL VDSKNFDDYM KSLGVGFATR QVASMTKPTT IIEKNGDILT LKTHSTFKNT EISFKLGVEF DETTADDRKV KSIVTLDGGK LVHLQKWDGQ ETTLVRELID GKLILTLTHG TAVCTRTYEK EA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity > 95% by SDS-PAGE. Biological Activity Testing in progress. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 10mM PB,150 mM NaCl,1 mM DTT, 0.1 % tween-20, 5 % trehalose, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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FGF-10, also known as Fibroblast Growth Factor-10, is a growth factor that belongs to the fibroblast growth factor family. It plays a crucial role in the development and repair of various tissues, particularly in the respiratory and limb development. Product Properties Synonyms FGF-10, Fibroblast growth factor 10, Keratinocyte growth factor 2 Uniprot No. O15520 Source E.coli-derived human FGF-10 protein, Gln38-Ser208, with C-terminal his tag Molecular Weight Approximately 20.4 kDa. Purity > 95% as determined by SDS-PAGE. Biological Activity Human FGF-10, his tag immobilized on CM5 chip can bind human FGFR2 alpha(IIIb) with an affinity constant of 9.69 x 10 -9 M as determined in a SPR assay (Biacore 8K). Endotoxin < 1 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 to ensure the concentration is greater than 100 ug/mL.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.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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FGF-19 is a member of the fibroblast growth factor (FGF) family. After being secreted from the intestine, FGF19 can enter the liver with the circulation and bind to FGFR4 in the liver to act. It has a hormone-like effect and plays an important role in metabolic regulation, such as regulating bile acid metabolism, regulating gallbladder filling, and improving blood glucose. Notably, aberrant expression of FGF19/FGFR4 promotes HCC development and metastasis.   Product Properties Synonyms FGF19;Fibroblast growth factor 1 Uniprot No. O95750 Source Recombinant Human FGF-19 Protein is expressed from HEK293 Cells with Flag tag at the N-terminal. It contains Leu 25-Lys 216. Molecular Weight The protein has a predicted MW of 23.36 kDa. And it migrates as 25-30 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 150 ng/mL. 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.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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The fibroblast growth factor-4 (FGF-4) gene was identified as HST-1 gene from human stomach cancers and Kaposi’ s sarcoma by a NIH3T3 transforming assay. FGF-4 has pleiotropic roles in many cell types and tissues, it is a mitogenic, angiogenic and survival factor, which is involved in cell proliferation and differentiation and in a variety of development processes.   Product Properties Synonyms HST, HST-1, HSTF-1, HBGF-4, Transforming Protein KS3, KFGF Uniprot No. P08620 Source E.coli-derived human FGF-4, Ser54-Leu206. Molecular Weight Approximately 16.8 kDa. Purity > 95% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with PBS to ensure the concentration is greater than 100ug/mL.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.   Notes 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Human FGF-9 protein, also known as fibroblast growth factor 9, is a member of the fibroblast growth factor (FGF) family. It functions as a signaling molecule, regulating various cellular processes like cell proliferation, differentiation, and migration. FGF-9 protein plays a vital role in various physiological and pathological processes, making it an important focus of research in the field of molecular biology and medicine.   Product Properties Synonyms FGF9, FGF-9, Glia-activating factor, GAF, glia-activating factor, HBFG-9, HBGF-9 Uniprot No. P31371 Source E.coli-derived human FGF-9 protein, Leu4-Ser208, with C-terminal His tag. Molecular Weight Approximately25.2kDa. Purity > 90% as determined by SDS-PAGE. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Liquid in PBS，the concentration is 0.3 mg/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.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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Fibroblast growth factor 12 (FGF12) is a fibroblast growth factor homologous factor, a subset of the FGF superfamily. Human FGF-12 is synthesized as a 243 aa protein. In human Vascular smooth muscle cells (VSMCs), FGF12 expression was inhibited at the transcriptional level by platelet-derived growth factor-BB. FGF12 inhibited cell proliferation through the p53 pathway and upregulated the key factors involved in VSMC lineage differentiation, such as myocardin and serum response factor. In addition, FGF12 and other FGF11 subfamily members do not activate any fibroblast growth factor receptors (FGFRs), although they can bind to heparin with high affinity like other FGFs. FGF12 has structural similarity with FGF1 and FGF2, in that it lacks a classical signal sequence and con-tains a nuclear localization signal, resulting in the accu-mulation of FGF12 in the nucleus without any release from cells.   Product Properties Synonyms FGF12, FGF-12, FGF12B, FHF1, FHF-1, fibroblast growth factor 12, fibroblast growth factor 12 Accession NP_00410 GeneID 2257 Source E.coli-derived human FGF-12 protein, Met1-Thr181. Molecular Weight Approximately 20.5 kDa. AA Sequence MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity >98% by SDS-PAGE and HPLC analyses Biological Activity The biological activity was determined by its binding ability in a functional ELISA. Immobilized recombinant human FGF R4/Fc Chimera at 5 µg/mL (100 µL/well) can bind recombinant human FGF-12 with a linear range of 1.6-100 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, pH7.4, with 1 mM DTT. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor 13 (FGF13), a member of the FGF11 subfamily, is a kind of intracrine protein similar to other family members including FGF11, FGF12, and FGF14. Unlike classical FGF, FGF13 exerts its bioactivities independent of fibroblast growth factor receptors (FGFRs). FGF13, a nonsecretory protein of the FGF family, is expressed in cerebral cortical neurons during development and is a candidate gene for syndromal and nonspecific forms of X-chromosome-linked mental retardation. The FGF-13 regulates glioma cell invasion and is important for bevacizumab-induced glioma invasion. FGF-13 plays a crucial role in neuron polarization and migration in the cerebral cortex. In mouse FGF-13 RNA was detected in developing central nervous system in cells, and was also found throughout the peripheral nervous system.   Product Properties Synonyms FGF13, FGF-13, FHF-2 Accession Q92913 GeneID 2258 Source E.coli-derived human FGF-13 protein, Met1-Thr245. Molecular Weight Approximately 27.6 kDa. AA Sequence MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Testing in process Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, pH 8.5, 500 mM NaCl Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor-16 (FGF16) is a member of FGF9 subfamily. All FGF family members are heparin-binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. FGF-16 is most similar to FGF-9, sharing 73% aa sequence homology. Human FGF-16 shares 99% and 98.6% aa sequence identity with the mouse and rat FGF-16, respectively. FGF-16 binds to and activates FGF receptor 4. The expression pattern of FGF-16 and its effect on adipocyte proliferation suggest a role for this protein on the proliferation of embryonic brown adipose tissue. FGF16 belongs to the large FGF family, which plays key role in promoting mitosis and cell survival, and also involved in embryonic development, cell growth, tissue repair, morphogenesis, tumor growth, and invasion. Meanwhile, the expression of FGF-16 in the perinatal and postnatal heart and its functional significance in neonatal rat cardiac myocytes.   Product Properties Synonyms FGF16, FGF-16, fibroblast growth factor 16 Accession O43320 GeneID 8823 Source E.coli-derived human FGF-16 protein, Ala2-Arg207. Molecular Weight Approximately 23.6 kDa AA Sequence AEVGGVFASL DWDLHGFSSS LGNVPLADSP GFLNERLGQI EGKLQRGSPT DFAHLKGILR RRQLYCRTGF HLEIFPNGTV HGTRHDHSRF GILEFISLAV GLISIRGVDS GLYLGMNERG ELYGSKKLTR ECVFREQFEE NWYNTYASTL YKHSDSERQY YVALNKDGSP REGYRTKRHQ KFTHFLPRPV DPSKLPSMSR DLFHYR Tag None Physical Appearance Sterile Colorless liquid. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 10 6 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 20 mM Tris-HCl, 1 M NaCl, pH 9.0, with 0.02 % Tween-20, 10 % Glycerol.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -70℃ for 6 months. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor-17( FGF17) is one of the fibroblast growth factor( FGF) family members and it makes up FGF8 subfamily along with FGF8 and FGF18. Mature human FGF- 17 shares 99% aa identity with mouse, rat, porcine and canine FGF- 17. The FGF domain of FGF- 17 shares the most aa identity with FGF- 8 (~75%) and FGF- 18 (~64%). Among different members of the FGF family, FGF17 and FGF8 share high sequence homology and have similar patterns of expression during embryogenesis. FGF- 17 is also expressed in adult bovine ovarian follicles and the human prostate, and its expression is increased by both benign hypertrophy and cancer of the prostate.   Product Properties Synonyms FGF17, FGF-17, fibroblast growth factor 17 Accession O60258 GeneID 8822 Source E.coli-derived human FGF-17 protein, Thr23-Thr216, with an N-terminal Met. Molecular Weight Approximately 22.6 kDa AA Sequence MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 10 5 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor-21 (FGF-21) belongs to the large FGF family which is encoded by the FGF-21 gene. Mature human FGF-21 shows 81% aa identity to mouse FGF-21, and is known to be active on mouse cells. The c-DNA for FGF-21 predicts a 209 aa polypeptide that contains a 28 aa signal sequence and a 181 aa mature region. FGF21 is a metabolic regulator that provides efficient and durable glycemic and lipid control in various animal models. And the FGF21 is a liver-derived endocrine factor that stimulates glucose uptake in adipocytes. Pharmacologic studies show that FGF21 has broad metabolic actions in obese rodents and primates that include enhancing insulin sensitivity, decreasing triglyceride concentrations, and causing weight loss.   Product Properties Synonyms FGF21, FGF-21, fibroblast growth factor 2 Accession Q9NSA1 GeneID 26291 Source E.coli-derived human FGF-21 protein, His29-Ser209 Molecular Weight Approximately 19.4 kDa. AA Sequence HPIPDSSPLL QFGGQVRQRY LYTDDAQQTE AHLEIREDGT VGGAADQSPE SLLQLKALKP GVIQILGVKT SRFLCQRPDG ALYGSLHFDP EACSFRELLL EDGYNVYQSE AHGLPLHLPG NKSPHRDPAP RGPARFLPLP GLPPALPEPP GILAPQPPDV GSSDPLSMVG PSQGRSPSYA S Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2.0 × 10 3 IU/mg in the presence of 5 µg/ml of recombinant mouse Klotho-β and 10 μg/ml of heparin. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Fibroblast growth factor 23 (FGF- 23) is a member of the FGF family, within a subfamily that also includes FGF- 19 and FGF- 21. FGF proteins contain a 120 amino acid (aa) core FGF domain that exhibits a beta-trefoil structure. β-Klotho has been identified as co-factor required for FGF-19, 21, 23 signaling. It can obviously increase ligand-receptor affinity. Klotho has a restricted distribution that limits FGF- 23 activity. FGF- 23 is produced by osteocytes and osteoblasts in response to high circulating phosphate levels, elevated parathyroid hormone, and circulatory volume loading. It functions as an endocrine phosphatonin by suppressing circulating phosphate levels. FGF- 23 interaction with renal proximal tubular epithelium decreases the renal resorption of phosphate by down-regulating phosphate transporters and by suppressing vitamin D production. It also decreases the intestinal absorption of phosphate.   Product Properties Synonyms ADHR,HPDR2, HYPF Accession Q9GZV9 GeneID 8074 Source E.coli-derived Human FGF-23, Thr25-Ile227. Molecular Weight Approximately 25.3 kDa. AA Sequence YPNASPLLGS SWGGLIHLYT ATARNSYHLQ IHKNGHVDGA PHQTIYSALM IRSEDAGFVV ITGVMSRRYL CMDFRGNIFG SHYFDPENCR FQHQTLENGY DVYHSPQYHF LVSLGRAKRA FLPGMNPPPY SQFLSRRNEI PLIHFNTPIP RRHTRSAEDD SERDPLNVLK PRARMTPAPA SCSQELPSAE DNSPMASDPL GVVRGGRVNT HAGGTGPEGC RPFAKFI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/mL, corresponding to a specific activity of > 2.0 × 10 3 IU/mg in the presence of 0.3 μg/mL of rMuKlotho and 10 μg/mL of heparin. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4 Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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The cytokine Fms-like tyrosine kinase 3 ligand (FLT3L), also known as Flt-3 Ligand, is an important regulator of hematopoiesis. Its receptor, Flt3, is expressed on myeloid, lymphoid and dendritic cell progenitors and is considered an important growth and differentiation factor for several hematopoietic lineages. Activating mutations of Flt3 are frequently found in acute myeloid leukemia (AML) patients and associated with a poor clinical prognosis. Mature human Flt- 3L consists of a 158 amino acid (aa) extracellular domain (ECD) with a cytokine-like domain and a juxtamembrane tether region, a 21 aa transmembrane segment, and a 30 aa cytoplasmic tail. At the amino acid sequence level, human and mouse FL are approximately 72% identical and the two proteins exhibit cross-species activity. The Flt3-L manifests antitumor activity, presumably due to its capacity to recruit dendritic cells and cause their proliferation.   Product Properties Synonyms Flt3-Ligand, FL, FLG3L, Flt3L, SL Cytokin Accession P49771 GeneID 2323 Source E.coli-derived human IL-1alpha protein, Thr27-Ala181. Molecular Weight Approximately 17.6 kDa. AA Sequence TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human AML5 cells is less than 1.0 ng/mL, corresponding to a specific activity of > 1.0 × 10 6 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 7.0. 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.   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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Fms-like tyrosine kinase 3 ligand (Flt-3 Ligand) is a cytokine that promotes differentiation of a variety of hematopoietic cells. Flt3L can increase the number of immune cells by activating hematopoietic progenitor cells.   Product Properties   Synonyms FLT3LG;FL;FLT3L Source Recombinant Human Flt3-Ligand Protein is expressed from HEK293 Cells with His tag at the N-terminal. It contains Thr27-Pro184. Endotoxin < 0.1 EU per μg by the LAL method. Purity > 95% by SDS-PAGE analyses. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS.   Storage    The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions   1. Please operate with lab coats and disposable gloves,for your safety.        2. This product is for research use only.  

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Follistatin (FS) was initially identified as a follicle-stimulating hormone inhibiting substance found in ovarian follicular fluid. It has since been shown that FS is a high‑affinity activin-binding protein that can act as an activin antagonist. Two alternatively spliced follistatin mRNAs, encoding mature FS with 288 amino acid (aa) residues (FS‑288) and 315 aa residues (FS‑315), exist. Natural FS purified from porcine ovaries is primarily a carboxy-terminal truncated form of FS‑315 composed of 300 aa residues. Cell surface-associated FS has been suggested to play a role in the clearance and bioavailability of activin in vivo. Besides activin, FS has also been shown to bind with multiple BMPs and to inhibit BMP activity in early Xenopus embryos. FS deficient mice have been shown to have multiple embryonic defects that will result in death shortly after birth. Product Properties Synonyms FS; FSActivin-binding protein; FST Accession P19883 GeneID 10468 Source E.coli-derived Human Follistatin, Gly30-Asn317. Molecular Weight Approximately 31.5 kDa. AA Sequence GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEEDVNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses. Biological Activity Testing in Progress. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 20mM Tris-HCl, pH 8.5, 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℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles. Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q. Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession P78423 GeneID 6376 Source E.coli-derived Human Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.6 kDa. AA Sequence QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD AMQHLDRQAA ALTRNG 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 of 5.0-10 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, 50 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.   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 FZD10 /Frizzled-10 Protein-VLP C230743E 20 μg C230743S 100 μg C230743M 100 μg C230743L 1 mg   Product Properties   Synonyms CD184,Fusin,D2S201E,FB22,HM89,HSY3RR,LAP3,LCR1,LESTR,NPY3R Source HEK293 Cells AA sequence Accession #Q9ULW2: Met1 - Val581 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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  Name Catalog No. Size Recombinant Human FZD7/Frizzled-7 Protein-VLP C230744E 20 μg C230744S 100 μg C230744M 100 μg C230744L 1 mg   Product Properties   Synonyms FZD7,Frizzled-7,FzE3,Fz-7,hFz7 Source HEK293 Cells AA sequence Accession #O75084: Met1 - Val574 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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Galectin-1, a polypeptidic factor that can have major effects on cell growth and apoptosis, is an important regulator of leukocyte function and tumor angiogenesis. Galectin-1 belongs to a family of 15 structurally related β-galactoside binding proteins that are able to control a variety of cellular events, including cell cycle regulation, adhesion, proliferation, and apoptosis. Human Galectin-1 shares 88% aa sequence identity with mouse, equine and ovine, 90% with rat, and 87% with bovine and porcine  Galectin-1. Recombinant human galectin-1 to three porphyrin compounds: Zn-porphyrin (ZnTPPS); Mn-porphyrin and Au-porphyrin. These compounds are widely applied in the photodynamic therapy of cancer. Galectin-1 can also modulate cell-cell and cell-matrix interactions.   Product Properties Synonyms Beta-galactoside-binding lectin L-14-I, BHL, DKFZp686E23103, GAL1, gal-1, Galaptin, galectin 1, Galectin1, Galectin-1, GBP, HBL, HLBP14, HPL, L-14, Lactose-binding lectin 1, LGALS1 Accession P09382 Source E.coli-derived Human Galectin-1, Ala2-Asp135. Molecular Weight Approximately 14.6 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE  analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human blood monocytes is in a concentration range of 1.0-10 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 solution in PBS, pH 7.4, with 1 mM DTT. 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 -25~-15℃ for 1 year. 1 months, 2 ~8℃ 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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Galectin-3, is classified as a chimeric member of the Galectin superfamily. Nuclear Galectin-3 can modulate gene expression, while cytosolic Galectin-3 can inhibit apoptosis. Galectin-3 contributes to the innate immune response against Candida albicans and Streptococcus pneumoniae, and it can facilitate acute inflammatory responses via neutrophil activation and opsonization, macrophage recruitment, and mast cell activation.   Product Properties Synonyms AGE-R3, CBP35, GAL3, L29, LGALS3, Mac-2 Accession P17931 Source Yeast-derived Human Galectin-3, Ala2-Ile250. Molecular Weight Approximately 26.0 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90% by SDS-PAGE  analyses. Biological Activity Recombinant human Galectin-3 is able to agglutinate red blood cells at a minimumeffective concentration of 25ug/ml. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in 1 × PBS, pH 7.4, 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. 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 products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 months, 2 ~8℃ 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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(C-X-C motif) ligand (CXCL)10 (CXCL10), also known as IP-10, belongs to the ELR(-) CXC subfamily chemokine. CXCL10 was originally identified as an IFN-gamma -inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that CXCL10 mRNA is also induced by LPS, IL-1 beta, TNF- alpha, IL-12 and viruses. CXCL10 was originally identified as an IFN-gamma -inducible gene in monocytes, fibroblasts and endothelial cells. CXCL10/IP-10 exerts its function through binding to chemokine (C-X-C motif) receptor 3 (CXCR3), a seven trans-membrane receptor coupled to G proteins. CXCL10/IP-10 and its receptor, CXCR3, appear to contribute to the pathogenesis of many autoimmune diseases, organ specific (such as type 1 diabetes, autoimmune thyroiditis, Graves' disease and ophthalmopathy), or systemic (such as rheumatoid arthritis, psoriatic arthritis, systemic lupus erythematosus, mixed cryoglobulinemia, Sjögren syndrome, or systemic sclerosis). In adition, CXCL10 has been reported to be a potent inhibitor of angiogenesis and to display a potent thymus-dependent antitumor effect.     Product Properties Synonyms Gamma-IP10, Small-inducible Cytokine B10 Accession P02778 GeneID 3627 Source E.coli-derived Human IP-10/CXCL10, Val22-Pro98. Molecular Weight Approximately 8.6 kDa AA Sequence VPLSRTVRCT CISISNQPVN PRSLEKLEII PASQFCPRVE IIATMKKKGE KRCLNPESKA IKNLLKAVSK EMSKRSP 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 peripheral blood neutrophils is in a concentration range of 10-50 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, 50 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.   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 GCGR/Glucagon receptor Protein-VLP C230745E 20 μg C230745S 100 μg C230745M 100 μg C230745L 1 mg   Product Properties   Synonyms Glucagon R, GCGR,Glucagon receptor Source HEK293 Cells AA sequence Accession #P47871: Met1 - Phe477 Endotoxin < 1EU per μg by the LAL method Purity >85% as determined by DLS Formulation 115mM Gly 4% trehalose Activity ELISA Data: Immobilized Human GCGR VLP at 5 ug/mL (30 uL/well) can bind Monoclonal Anti-Human GCGR antibody, The EC50 was approximately 0.009199 µg/ml. Applications ELISA, Kinetics (BLI), Kinetics (SPR), Immunization Dilution Dilute with PBS   Figure Figure 1.  Immobilized Human GCGR VLP at 5 ug/mL (30 uL/well) can bind Monoclonal Anti-Human GCGR antibody, The EC50 was approximately 0.009199 µg/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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