TNF-alpha (human) (multimeric) (Recombinant)

Source :HEK 293 cells Specific Binds to human and mouse TNF-R1 and TNF-R2.Tumor necrosis factor (TNF, cachexin or cachectin and formerly known as tumor necrosis factor-alpha) is a cytokine involved in systemic inflammation and is a member of a group of cytokines that stimulate the acute phase reaction. MultimericTNF-alpha(TM) is a high activity construct in which two trimeric TNF-alpha ligands are artificially linked via the collagen domain of ACRP30. The receptor TNF-R1 is activated by both the membrane-bound and soluble trimeric forms of TNF-alpha, whereas the receptor TNF-R2 only responds to the membrane-bound form of TNF-alpha (TNF-alpha (human) (multimeric) (rec.) (32-190048). Since the MultimericTNF-alpha(TM) mimics the membrane-bound form (forms oligomers higher than trimer), it is the only TNF-alpha protein that can activate the TNF-R2. For TNF-R1 activation, either "normal" TNF-alpha or MultimericTNF-alpha(TM) can be used. Protein function: Cytokine 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. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6. [The UniProt Consortium]