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C036
Recombinant Human TNFa/TNFSF2 (high active)
10ug
800
720
现货
国产
-
C036
Recombinant Human TNFa/TNFSF2 (high active)
50ug
2320
2088
现货
国产
-
C036
Recombinant Human TNFa/TNFSF2 (high active)
500ug
9640
8676
现货
国产
-
C036
Recombinant Human TNFa/TNFSF2 (high active)
1mg
13760
12384
现货
国产
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Catalog# C036 Source E.coli 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 Accession # P01375 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. References Wu Y,et al.DDIT3 overexpression increases odontoblastic potential of human dental pulp cells
PMID:24738922
http://www.ncbi.nlm.nih.gov/pubmed/24738922