Dibasic endoprotease, also known as Kex2 protease or YSCF protease, is responsible for processing the precursors of killer toxin and α-factor in yeast. It is a calcium-dependent serine protease that specifically recognizes and cleaves peptide bonds at the carboxyl terminus of dibasic amino acid pairs such as Arg-Arg and Lys-Arg. Unlike trypsin, Kex2 cannot recognize or cleave peptide bonds at the carboxyl terminus of single basic amino acids (i.e., arginine or lysine). The activity of Kex2 protease is not inhibited by conventional serine protease inhibitors such as aprotinin, PMSF, or TPCK.
Yeasen recombinant Kex2 protease is expressed in Pichia pastoris, contains no animal-derived components, and is free from animal-derived viral contamination. It possesses the same enzymatic specificity as the native Saccharomyces cerevisiae Kex2 protease. The optimal pH for activity is pH 9.0, and the stable storage pH range is 5.0-6.0.
This Yeasen recombinant Kex2 protease is supplied in liquid form at a concentration of 1 mg/mL, ready for immediate use. Additionally, Yeasen also offers recombinant Kex2 protease in lyophilized powder form (Cat#20418ES), which can be stored at 2-8°C.