protein

TNF-alpha/TNFSF2 Protein, Human (HEK293, His)

HY-P78527A

2 μg;10 μg;50 μg;100 μg;500 μg

35;60;165;280;785 USD

TNF-alpha/TNFSF2 Protein, Human (HEK293, His)

proteins

HEK293

2 μg;10 μg;50 μg;100 μg;500 μg

35;60;165;280;785 USD

TNF-α/TNFSF2 protein is a macrophage-secreted cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR, inducing tumor cell death and acting as a pyrogen. It is associated with cachexia and stimulates cell proliferation and differentiation. TNF-alpha/TNFSF2 Protein, Human (HEK293, His) is the recombinant human-derived TNF-alpha/TNFSF2 protein, expressed by HEK293 , with C-His labeled tag. The total length of TNF-alpha/TNFSF2 Protein, Human (HEK293, His) is 157 a.a., with molecular weight of ~17 kDa.

Human

The TNF-alpha/TNFSF2 Protein, a cytokine, binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR, primarily secreted by macrophages with the capability to induce cell death in specific tumor cell lines. Acting as a potent pyrogen, it causes fever through direct action or by stimulating interleukin-1 secretion and is implicated in the induction of cachexia. Furthermore, under specific conditions, TNF-alpha can stimulate cell proliferation and induce cell differentiation. Notably, in individuals with rheumatoid arthritis, it impairs regulatory T-cells (Treg) function via FOXP3 dephosphorylation, up-regulating the expression of protein phosphatase 1 (PP1) that dephosphorylates the key 'Ser-418' residue of FOXP3, rendering Treg cells functionally defective. Additionally, TNF-alpha is a key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. It induces insulin resistance in adipocytes by inhibiting insulin-induced IRS1 tyrosine phosphorylation and glucose uptake, leading to GKAP42 protein degradation and TNF-induced insulin resistance. Furthermore, it plays a role in angiogenesis by synergistically inducing VEGF production with IL1B and IL6, and it promotes osteoclastogenesis, contributing to bone resorption. Lastly, the TNF intracellular domain (ICD) form induces IL12 production in dendritic cells, highlighting its diverse impact across various physiological processes.

NF-alpha; TNF; TNFA; Tumor necrosis factor

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.