|Recombinant Human Tumor Necrosis Factor-α/TNF-α High Active Mutant|
|Description||Recombinant Human TNF Alpha, Tumor Necrosis Factor-α/TNF-α Mutant produced in E. coli is a single non-glycosylated polypeptide chain containing 151 amino acids with a molecular mass of 16,886 Daltons.|
|Names||Recombinant Human TNF Alpha, Tumor Necrosis Factor, Cachectin, TNF-Alpha, Tumor Necrosis Factor Ligand Superfamily Member 2, TNF-a, TNF, TNFA, TNFSF2|
|Formulation||Lyophilized from a 0.2 μM filtered solution of 20mM PB, 150mM NaCl, pH 7.4|
|Shipping||The product is shipped at ambient temperature.|
|Reconstitution||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 1X PBS.
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.
|Biological Activity||ED50 is less than 0.01 ng/ml as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.|
Specific Activity of 1.0 x 108 IU/mg.
|Purity||Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.|
|Endotoxin||Less than 0.1 ng/μg (1 IEU/μg).|
|Background||Recombinant Human TNF Alpha: 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.|