Recombinant Human TNF alpha (C-6His)
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.
Description
| Reference | ESCIT101 |
|---|---|
| Size | 10ug |
| Molecular Weight | 18.5 KDa |
| Purity | Greater than 95% as determined by reducing SDS-PAGE. |
| Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
| Biological Activity |
Other names: Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF-a; TNF; TNFA; TNFSF2
Redissolve: Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100?g/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
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-? (TNF-?) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-? while cells that express CD8 secrete little or no TNF-?. Synthesis of TNF-? can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF-? has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hESCIatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-? mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF-? 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-?, which binds to both murine TNF recESCItors. Based on these results, many TNF-? 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-? 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.