Recombinant Human Tumor necrosis factor/TNFA is produced with our E. coli expression system. The target protein is expressed with sequence (Gly57-Leu233) of Human TNFA fused with a 6His tag at the N-terminus.
Pureté
> 95 % as determined by reducing SDS-PAGE.
Stérilité
0.2 μm filtered
niveau d'endotoxine
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
TNF alpha
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
TNF alpha
Origine: Humain
Hôte: Yeast (Pichia pastoris)
> 97 % by SDS-PAGE.
Active
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
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.
Buffer
Lyophilized from a 0.2 μm filtered solution of 20 mM PB,100 mM NaCl, pH 7.2.
Conseil sur la manipulation
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Stock
4 °C/-20 °C/-80 °C
Stockage commentaire
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.
Tumor Necrosis Factor-alpha (TNF-alpha) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-alpha while cells that express CD8 secrete little or no TNF-alpha. Synthesis of TNF-alpha can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF-alpha has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-alpha mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF-alpha 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-alpha, which binds to both murine TNF receptors. Based on these results, many TNF-alpha 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-alpha 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. Alternative Names: Tumor Necrosis Factor, Cachectin, TNF-Alpha, Tumor Necrosis Factor Ligand Superfamily Member 2, TNF-a, TNF, TNFA, TNFSF2