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

TNF-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 proteolytically cleaved to yield a soluble, biologically active, 17kD TNF-α, which forms a non-covalently linked homotrimer in solution.

Recombinant Human TNF-α is a soluble 157 amino acid protein (17.4kD) which corresponds to C-terminal extracellular domain of the full length transmembrane protein.

Recombinant protein corresponding to human TNF-alpha expressed in E. coli.

Biological Activity:
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomyocin D is <0.05ng/ml, corresponding to a specific activity of >2x10e7units/mg.

Amino Acid Sequence:
VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIAL

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.