TNF-alpha, Recombinant, Mouse, Animal Free (Tumor Necrosis Factor, TNFSF2, Cachectin, Differentiation-inducing Factor, DIF, Necrosin, Cytotoxin)

NF-α is a pleiotropic pro-inflammatory cytokine secreted by various cells, including adipocytes, activated monocytes, macrophages, B cells, T cells and fibroblasts. It belongs to the TNF family of ligands, and signals through two receptors, TNFR1 and TNFR2. TNF-α is cytotoxic to a wide variety of tumor cells, and is an essential factor in mediating the immune response against bacterial infections. TNF-α also plays a role in the induction of septic shock, autoimmune diseases, rheumatoid arthritis, inflammation, and diabetes. Human and murine TNF-α demonstrate significant cross-species reactivity. TNF-α exists in two forms; a type II transmembrane protein, and a mature soluble protein.

The TNF-α transmembrane protein is proteolitically cleaved to yield a soluble, biologically active, 17kD TNF-α, which forms a non-covalently linked homotrimer in solution.

Recombinant protein corresponding to mouse TNF-alpha, a soluble 157 amino acid protein (17.3kD) which corresponds to C-terminal extracellular domain of the full length transmembrane protein, expressed in E. coli.

Biological Activity:
Determined by the cytolysis of murine L929 cells in the presence of Actinomyocin D. The expected ED50 is <0.1ng/ml, corresponding to a specific activity of >1x10e7units/mg.

Amino Acid Sequence:
MLRSSSQNS SDKPVAHVV ANHQVEEQL EWLSQRANA LLANGMDLK DNQLVVPAD GLYLVYSQV LFKGQGCPD YVLLTHTVS RFAISYQEK VNLLSAVKS PCPKDTPEG AELKPWYEP IYLGGVFQL EKGDQLSAE VNLPKYLDF AESGQVYFG VIAL

Protein Content:
Verified by UV Spectroscopy and/or SDS-PAGE gel.

Storage and Stability:
Lyophilized and reconstituted products are stable for 6 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.