TNF-α, a versatile pro-inflammatory cytokine, is produced by various cell types such as adipocytes, activated monocytes, macrophages, B cells, T cells, and fibroblasts. It belongs to the TNF ligand family and interacts with two receptors, TNFR1 and TNFR2. Its functions include cytotoxicity against numerous tumor cells and essential involvement in the immune response against bacterial infections. TNF-α is also implicated in septic shock, autoimmune conditions, rheumatoid arthritis, inflammation, and diabetes. Both human and murine TNF-α exhibit substantial reactivity across species.
Structurally, TNF-α exists in two forms: a type II transmembrane protein and a mature soluble protein. The transmembrane protein undergoes proteolytic cleavage to generate a biologically active 17 kDa TNF-α, forming a non-covalently linked homotrimer in solution. Recombinant Human TNF-α is a soluble 157 amino acid protein (17.4 kDa) representing the C-terminal extracellular domain of the full-length transmembrane protein.
$200.00 – $1,500.00
Product Specifications
Species Human
Published species
Dog, Human, Mouse, Pig, Rat, Virus
Expression System E. coli
Amino acid sequence
VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIAL
Molecular weight 17.4 kDa
Class Recombinant
Type Protein
Purity
≥ 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin concentration <0.1 EU/µg
Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomyocin D is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 10^7 units/mg.
Conjugate Unconjugated
Form Lyophilized
Contains
no preservative
Storage conditions -20°C
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