Recombinant Kex2 Protease

Kex2 protease is a membrane-bound, Ca²⁺-dependent serine protease that belongs to the subtilisin family and functions as an endogenous proprotein processing enzyme natively encoded in yeast. It specifically recognizes and cleaves peptide bonds at the carboxy-terminal side of dibasic amino acid motifs, including Arg-Arg, Lys-Arg, and Pro-Arg sequences; unlike trypsin, Kex2 does not recognize or cleave isolated single basic residues, i.e., individual arginine or lysine residues. This recombinant Kex2 product is produced via heterologous expression in Pichia pastoris, carries a His-tag, exhibits catalytic activity across a pH range of 7.0–9.0 with an optimal reaction temperature of 37 °C, retains high stability under mildly acidic conditions (pH 5.0–6.0), and unlike conventional serine proteases, its activity is not inhibited by inhibitors such as aprotinin, PMSF, and TPCK.