Kex-2 protease specifically recognizes and cleaves the carboxy-terminal peptide bond of dibasic amino acids such as Lys-Arg/X and Arg-Arg/X.

Kex2 protease is a membrane-bound, Ca2+-dependent serine protease that can specifically recognize and cleave the carboxy-terminal peptide bonds of dibasic amino acids such as Arg-Arg, Lys-Arg, and Pro-Arg. It belongs to the subtilisin family and is a precursor processing enzyme encoded by yeast itself. Unlike trypsin, Kex2 cannot recognize and cleave the carboxyl-terminal peptide bond of a single basic amino acid, namely arginine or lysine. This product is expressed and produced by Pichia pastoris, has His-tag, and the reaction pH is 7.0-9.0. The optimal reaction temperature is 37℃‌. Stable in an acidic environment (pH 5.0-6.0). Kex2 protease activity is not inhibited by conventional serine protease inhibitors such as aprotinin, PMSF, and TPCK.

1. Enzymatic hydrolysis of proteins, peptide map analysis, sequencing.

2. Can be used to cleave fusion tags and secreted peptides in yeast exogenous protein expression.

3. Kex2 combined with CPB is commonly used for the production and preparation of insulin analogs, GLP-1, and recombinant peptides.

1. High quality: high purity, high specific activity, no residue.

2. GMP production: GMP-grade products can be provided.

3. Customized specifications: specifications can be customized according to customer quality requirement.

4. Stable supply: Stable quality control and long-term supply.

Freeze-dried powder is stored at 2~8℃ and is valid for two years.

1. Due to the freezing and thawing of the protein causingpartial inactivation, after the first preparation of the storage solution of the corresponding concentration, it must be aliquoted and frozen at -20°C or lower to avoid repeated freezing and thawing.

2. Please refer to the relevant literature for the specific optimal working concentration orexplore and optimize it through experiments according to the purpose of the experiment and specific cells and animals.

3. Do not shake vigorously with vortex to avoid protein denaturation and inactivation.