TNF-alpha/TNFSF2 Protein, Human (HEK293)

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) is the recombinant human-derived TNF-alpha/TNFSF2 protein, expressed by HEK293, with tag free.

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.

1. Measured by its binding ability in a functional ELISA.Immobilized Human TNF-alpha at 1 μg/mL (100 μL/well) can bind Humira with a linear range of 0.1-2 ng/mL.
2. Human TNF-alpha, premium grade induces cytotoxicity effect on the WEHI-13VAR cells in the presence of the metabolic inhibitor actinomycin D. The specific activity of Human TNF-alpha is >2.00×10⁷ IU/mg, which is calibrated against human TNF-alpha WHO International Standard.
3. Measured in a cytotoxicity assay using L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED₅₀ for this effect is 53.51 pg/mL, corresponding to a specific activity is 1.87×10⁷ units/mg.

• 
  Measured in a cytotoxicity assay using L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED₅₀ for this effect is 53.51 pg/mL, corresponding to a specific activity is 1.87×10⁷ units/mg.

Human

HEK293

Tag Free

P01375 (V77-L233)

7124

Full Length of TNF soluble form

VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL

Approximately 14-20 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 11% trehalose.
2. Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.

<0.01 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.