Recombinant Human TNF-alpha/TNFA Protein (aa 57-233, His Tag) (PKSH033165)
For research use only.
| Synonyms | Cachectin, TNF, TNF-Alpha, TNF-a, TNFA, TNFSF2, Tumor Necrosis Factor, Tumor Necrosis Factor Ligand Superfamily Member 2 |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Gly57-Leu233 |
| Accession | P01375 |
| Calculated Molecular Weight | 21.8 kDa |
| Observed Molecular Weight | 18 kDa |
| Tag | N-His |
| Bio-activity | Measured in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is 30-150 pg/ml. |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation |
Lyophilized from a 0.2 μm filtered solution of 20mM PB, 100mM NaCl, pH 8.0. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
| 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 activities on tumor 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. |
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