| Description | Insulin, recombinant human (rHu) is identical in function and structure to the native human sequence. A hormone consisting of two polypeptide chains, rHu Insulin′s A-chain (21 amino acids) and B-chain (30 amino acids) are covalently linked by disulfide bonds between cysteine residues. This Insulin, recombinant human (rHu) is identical in function and structure to the native human sequence. A hormone consisting of two polypeptide chains, rHu Insulin′s A-chain (21 amino acids) and B-chain (30 amino acids) are covalently linked by disulfide bonds between cysteine residues. This genetically engineered human insulin is a full sequence molecule producted by recombinant DNA technology in baker′s yeast. Application:Serum-free medium supplements such as insulin are essential for long-term growth of commonly used mammalian cell lines. When insulin is absent from media, cell may exhibit disturbances in morphology and growth rate.Recombinant Human Insulin has been used in the media for adipogenic induction of mesenchymal stem cells. It has been used as a supplement in the cell culture media of airway epithelial cells. It has been used in the culture media for differentiation of cells, GLUT4 (glucose transporter type 4) translocation assay and to study interaction of insulin with insulin receptor via surface plasmon resonance... Read More | Inquire | Apatinib(YN-968D1) is an orally bioavailable, selective VEGFR2 inhibitor with IC50 of 1 nM | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis... Read More | Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the receptor XCR1, formally known as GPR5. The expression of lymphotactin is abundant in some activated T cells such as activated CD8+ T cells and other class I MHC restricted T cells. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. XCL1 induces its chemotactic function by binding to a chemokine receptor called XCR1. Recombinant Human XCL1 which is a single non-glycosylated polypeptide chains containing 92 amino acids and it shares approximately 60 % amino acid sequence homology with the murine and rat protein... Read More |