Recombinant Human TNF-alpha/TNFA Protein (aa 77-233, His Tag)(Active) | PKSH033164

Recombinant Human TNF-alpha/TNFA Protein (aa 77-233, His Tag)(Active) | PKSH033164 | Gentaur US, UK & Europe Disrtribition

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

Active Protein: Active protein

Activity: Recombinant Human Tumor Necrosis Factor alpha is produced by our E.coli expression system and the target gene encoding Val77-Leu233 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Human Tumor Necrosis Factor alpha is produced by our E.coli expression system and the target gene encoding Val77-Leu233 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

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

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

Stability and 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.

Molecular Mass: 18.5 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, pH 8.0.

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.

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