Recombinant Carboxypeptidase B
This recombinant carboxypeptidase B product is produced via microbial fermentation and heterologous expression in either Escherichia coli or Pichia pastoris, supplied without a His-tag fusion, and exhibits optimal catalytic activity at pH 7.5–9.0. It is ideally suited for manufacturing recombinant insulin and its analogs, GLP-1 receptor agonist therapeutics, and a broad range of other recombinant polypeptide products.
Product Details
Carboxypeptidase B (CPB), also known as peptidyl-L-lysine (L-lysine) hydrolase or protaminase, specifically catalyzes the release of C-terminal basic amino acid residues (lysine [K], arginine [R], histidine [H]) from polypeptide chains. This recombinant product is produced via microbial fermentation and heterologous expression in either Escherichia coli or Pichia pastoris, supplied without a His-tag fusion, and exhibits optimal catalytic activity across a pH range of 7.5–9.0; its activity is subject to competitive inhibition by free arginine and lysine, and is also potently inhibited by metal ion chelators such as EDTA.
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