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Recombinant Human TNF-alpha/TNFA Protein (His Tag)

Cat:PKSH033164
Manual MSDS

Price: $ 249

Price: $ 98

Size:
100μg 20μg
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  • Expression Host: E.coli
  • Accession: P01375
  • Applications: Cell culture
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Product Details
Synonyms Tumor Necrosis Factor;Cachectin;TNF-Alpha;Tumor Necrosis Factor Ligand Superfamily Member 2;TNF-a;TNF;TNFA;TNFSF2
Species Human
Expression Host E.coli
Sequence Val 77-Leu 233
Accession P01375
Calculated Molecular Weight 18.3 kDa
Observed Molecular Weight 17 kDa
Tag C-His
Bio-activity Measure by its ability to induce cytotoxicity in L929 cells in the presence of actinomycin D. The ED<sub>50</sub> for this effect is < 0.1 ng/mL. The specific activity of recombinant human TNF alpha is approximately ≥ 1 x 10<sup>7</sup> IU/mg.
Purity > 97 % as determined by reducing SDS-PAGE.
Endotoxin < 0.1 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile PBS,pH 8.0.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.
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.