Recombinant Human TNF/TNFa/TNFSF2(C-polyHis)
- 发布日期: 2017-06-23
- 更新日期: 2026-01-28
产品详请
| 产地 |
北京
|
| 品牌 |
solarbio
|
| 货号 |
P00162
|
| 保存条件 |
Lyophilized protein should be stored at < -20癈, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7癈 for 2-7 days. Aliquots of reconstituted samples are stable at < -20癈 for 3 months.
|
| 保质期 |
3个月个月
|
简介:Recombinant Human Tumor Necrosis Factor alpha is produced by our E.coli expression system and the target gene encoding Val77-Leu233 is expressed with a 6His tag at the C-terminus.
种属:Human
表达系统:E.coli
Endotoxin:Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test.
storage: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.
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.