Human TNF protein

• Catalog Number: orb594842
• Category: Proteins
• Description: Recombinant Human Tumor necrosis factor(TNF),partial (Active)
• Tag: N-terminal 6xHis-tagged
• Form/Appearance: Lyophilized powder
• Purity: Greater than 95% as determined by SDS-PAGE.
• MW: 21.8 kDa
• UniProt ID: P01375
• Protein Sequence: GPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
• Protein Length: Extracellular Domain
• Source: E.coli
• Biological Origin: Homo sapiens (Human)
• Biological Activity: The ED50 as determined in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D is less than 1 ng/ml.
• Expression Region: 57-233aa
• Endotoxins: Less than 1.0 EU/µg as determined by LAL method.
• Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
• Buffer/Preservatives: Lyophilized from a 0.2 μm filtered 20 mM PB, 100 mM NaCl, pH 7.2
• Alternative names: Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor
• Background: Tumor Necrosis Factor-α (TNF-α) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-α while cells that express CD8 secrete little or no TNF-α. Synthesis of TNF-α can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF-α has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-α mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF-α that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-α, which binds to both murine TNF receptors. Based on these results, many TNF-α mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic actitumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF-α High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo
• Note: For research use only
• Application notes: Extracellular Domain
• Expiration Date: 6 months from date of receipt.

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.