Recombinant Mouse TNF-alpha Protein (C09-1095-998)

Purity>97% (SDS-PAGE; HPLC). Purity is greater than 97% as determined by SEC-HPLC and reducing SDS-PAGE.Additional sequence informationNP_038721. Mature protein; soluble form.FunctionCytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation.Post-translationalThe soluble form derives from the membrane form by proteolytic processing. The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1. O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.Tumor necrosis factor alpha (TNF-α), also called Cachectin, is the best-know member of the TNF-family, which can cause cell death. This protein is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. Human and murine TNF-α show approximately 79 % homology at the amino acid level and cross-reactivity between the two species. Two types of receptors for TNF-α have been described and virtually all cell types studied show the presence of one or both of these receptor types. The recombinant Murine TNF-α is a non-glycosylated polypeptide chain containing 157 amino acids. Specifications and Purity: Animal Free, >97% (SDS-PAGE; HPLC ), Active, E.coli, No tag, 80-235aa .