Description_x000D_ Application_x000D_ Carboxypeptidase B has been used in a study to develop a non-invasive pregnancy assay for use in both captive and wild polar bears. Carboxypeptidase B has been used in a study that identified new potential biomarkers of acute pancreatitis._x000D_ The enzyme from Sigma has been used to develop homogeneous time-resolved fluorescence (HTRF) assay for measuring carboxypeptidase B activity in a miniaturized high-throughput screening format. It has been used to evaluate the impact of the C-terminal lysine(s) in human plasminogen binding to Bifidobacterium. The effect of treatment with carboxypeptidase B, which is a C-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis._x000D_ Packaging_x000D_ 1, 5 mg in glass bottle_x000D_ Biochem/physiol Actions_x000D_ Carboxypeptidase B is a proteolytic enzyme capable of rapidly hydrolyzing peptide bonds to release certain carboxyl-terminal basic amino acids from peptides and proteins. Its molecular mass is 34,300±600 Da. It contains one non-dialyzable gram atom of zinc per mole. The enzyme activity is inhibited by metal chelating agents 1, 10-phenanthroline, 8-hydroxyquinoline-5-sulfonic acid, and 2,2’-dipyridyl._x000D_ Packaging_x000D_ Package size based on protein content_x000D_ Unit Definition_x000D_ One unit will hydrolyze 1.0 μmole of hippuryl-L-arginine per min at pH 7.65 at 25 °C._x000D_ Physical form_x000D_ Contains HEPES buffer salts, zinc chloride and carbohydrate_x000D_ Preparation Note_x000D_ Treated with protease inhibitor, AEBSF, to eliminate serine protease activity._x000D_ Analysis Note_x000D_ Protein determined by biuret.