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Recombinant Human TNF-alpha/TNFA Protein (aa 57-233, His Tag)(Active) - PKSH033165
Recombinant Human TNF-alpha/TNFA Protein (aa 57-233, His Tag)(Active) - PKSH033165

Recombinant Human TNF-alpha/TNFA Protein (aa 57-233, His Tag)(Active) - PKSH033165

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Recombinant Human TNF-alpha/TNFA Protein (aa 57-233, His Tag)(Active)

Sizes: 10μg, 50μg

Catalogue Numbers: PKSH033165-10, PKSH033165-50

Citations, Manuals and MSDS Available upon request.

Abbreviation: TNF-alpha; TNFA

Target Symptom: Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF-a; TNF; TNFA; TNFSF2

Research Area: Signal Transduction; Cardiovascular; Cancer; immunology; metabolism;

Target Species: Human

Expression Host: E.coli

Application: Cell culture

Fusion Tag: N-6His

UNIProt ID: P01375

Accession: P01375

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.

Activity: Measured in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is 30-150 pg/ml.

Sequence: Gly57-Leu233

Purity: > 95 % as determined by reducing SDS-PAGE.

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB; 100mM NaCl, pH 7.2.
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.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Calculated MW: 21.8 kDa

Observed MW: 21 kDa

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.

Research Use Only