Recombinant Human TNF-Alpha protein

The clinical use of the potent antitumor activity of TNF-α has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-αmutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-α, which binds to the Mouse TNF-R55 but not to the Mouse TNF-R75, exhibits retained antitumor activity and reduced systemic toxicity in mice compared with Mouse TNF-α, which binds to both Mouse TNF receptors. Based on these results, many TNF-αmutants 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.

Approximately 16.9 kDa, a single non-glycosylated polypeptide chain containing 151 amino acids. Compared with the wild-type, rHuTNF-α Variant has an amino acid sequence (a.a.) deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg1 and Phe157 which is proven to have more activity and with less inflammatory side effect in vivo.