Description

• General description: The TNFα (tumor necrosis factor α) gene is mapped to human chromosome 6p21.33.[1] TNFα is a member of TNF superfamily.[2] TNF-α has a palmitoyl group in the cysteine residue and is phosphorylated in the transmembrane region serine residue.[3]
• Application: Tumor Necrosis Factor-α (TNF-α) human has been used In induction of netting neutrophils by anti-neutrophil cytoplasmic antibody and to study its effect on platelet activation and formation of monomeric C-reactive protein.[4]To study the effect of TNF-α on miR-221 and fractalkine expression.[5][6]To induce inflammatory cell responses.[7]In NF-κB luciferase reporter assay.[8]
• Biochem/physiol Actions: Tumor Necrosis Factor-α (TNF-α) is a potent pro-inflammatory cytokine that plays a role in the rheumatoid arthritis pathology,[3] psoriatic arthritis (PsA) and psoriasis.[15] It stimulates interleukins IL-1 and IL-6. Polymorphism in the TNF-α gene is associated with destructive arthropathy in PsA.[15] The post-translational modifications in TNF-a is crucial for its functionality.[3]
• Preparation Note: Tumor Necrosis Factor-α (TNF-α) is expressed in human HEK 293 cells and has been shown to be predominantly a glycosylated, non-covalently linked homotrimer with a molecular mass of 51 kDa (gel filtration). Production in human 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications.
• Analysis Note: The specific activity was determined by the dose-dependent cytotoxity of the TNF alpha sensitive cell line L-929 in the presence of actinomycin D.