Recombinant Human TNF-alpha/TNFSF2
Tumor necrosis factor alpha (TNF-α), also called cachectin, is the best-know member of the TNF-family, which can cause cell death. This protein is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. TNF-α occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Human and murine TNF-α show approximately 79 % homology at the amino acid level and cross-reactivity between the two species. Two types of receptors for TNF-α have been described and virtually all cell types studied show the presence of one or both of these receptor types.
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Alternate Names |
Tumor Necrosis Factor-alpha, Human TNF-α, rHuTNF-α/TNFSF2, Cachectin, Differentiation-inducing factor, DIF |
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Gene ID |
7124 |
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Accession # |
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AA Sequence |
MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA EAKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL |
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Molecular Weight |
Approximately 17.5 kDa, a single non-glycosylated polypeptide chain containing 158 amino acids. |
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Source |
Escherichia coli |
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Biological Activity |
Fully biologically active when compared to standard. The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg in the presence of actinomycin D. |
| Components | 10 μg | 50 μg | 100 μg | 1 mg |
| Recombinant Human TNF-alpha/TNFSF2 (1 mg/mL) | 10 μL | 50 μL | 100 μL | 1 mL |
Store the components at -20 °C. | ||||