Recombinant Human TNF-alpha Variant is a single non-glycosylated polypeptide chain containing 151 amino acids. Compared with the wild-type, this TNF-alpha Variant has an amino acid sequence (a.a.) deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157, which are proven to have more activity and with less inflammatory side effect in vivo.
Background: The clinical use of the potent antitumor activity of TNF-alpha has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-alpha mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-alpha, which binds to the mouse TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with moue TNF-alpha, which binds to both mouse 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 exhibited lower systemic toxicity in vivo.
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