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Kex2 protease is a precursor processing protease derived from Saccharomyces cerevisiae and expressed in yeast. As a calcium-dependent serine protease, it specifically recognizes and cleaves the carboxy-terminal peptide bonds of dibasic amino acids such as Arg‑Arg, Lys‑Arg, and Pro‑Arg.
Unlike trypsin, Kex2 does not recognize or cleave the carboxy-terminal peptide bonds of single basic amino acids (arginine or lysine). Its activity is not inhibited by common serine protease inhibitors including aprotinin, PMSF, and TPCK.
The optimal pH for catalysis is pH 9.0, and the stable storage pH range is pH 5.0–6.0.
Applications
（1）Enzymatic digestion of proteins and polypeptides.
（2）Commonly used in biopharmaceutical manufacturing in combination with CPB for the production of insulin analogs, GLP‑1, and recombinant polypeptides, such as insulin glargine and semaglutide.
Advantages
（1）High activity and strong specificity.
（2）No animal-derived components used in production.
（3）Excellent stability, facilitating transportation and storage.
Information
（1）Product Name: Recombinant Kex2 Protease
（2）Catalog No. : YJ-O-227
（3）Size: 0.1 mg / 0.5 mg / 1.0 mg
（4）Storage temperature: 2-8 ℃