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Recombinant Human Tumor Necrosis Factor-α/TNF-α High Active Mutant (C036)

目录 规格 价格
【TNFa/TNFSF2 (high active)产品说明】:
Recombinant Human Tumor Necrosis Factor alpha is produced by our E.coli expression system and the target gene encoding is expressed.
【TNFa/TNFSF2 (high active)质量控制】:
Measured by the cytolysis of murine L929 cells in the presence of Actinomycin D.
ED50 is less than 0.01 ng/ml. Specific Activity of 1.0 x 10^8 IU/mg.
Greater than 95% as determined by reducing SDS-PAGE.
【TNFa/TNFSF2 (high active)制剂】:
Lyophilized
【TNFa/TNFSF2 (high active)保存】:
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
【TNFa/TNFSF2 (high active)复溶】:
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
【关于TNFa/TNFSF2 (high active)】:
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.
For research use ONLY.