| 説明 |
TNF alpha Protein, Human, Recombinant (aa 57-233, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 18 KDa and the accession number is P01375. |
| Species |
Human
|
| Expression Host |
E. coli
|
| Tag |
N-6xHis
|
| Accession Number |
P01375
|
| 別名 |
TNFA, TNF-α, Cachectin, TNF-Alpha, TNF-a, TNF α, Tumor Necrosis Factor, TNFSF2, TNF, Tumor Necrosis Factor Ligand Superfamily Member 2
|
| Amino Acid |
Gly57-Leu233
|
| Construction |
Gly57-Leu233
|
| Protein Purity |
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
|
| 分子量 |
18 KDa (reducing condition)
|
| Endotoxin |
< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
|
| Formulation |
Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM PB, 100 mM NaCl, pH 8.0.
|
| Reconstitution |
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
|
| Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
|
| Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
|
| Research 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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