Package: Aluminum Foil Bag

Uses : Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides.

Product description: Sequencing Grade Carboxypeptidase B Animal Origin Free SOURCE Expressed in E. Coli, purified by HPLC. DESCRIPTION Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0. Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation. MAIN FEATURES Source E.Coli Purified by HPLC Physical form White or white-like lyophilized powder Specific activity NLT 200 units/mg pro. No Contaminant activity No trypsin, chymotrypsin, carboxypeptidase A, or other proteases contaminant. APPLICATION Protein structure and sequence analysis, such as hydrolyze basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. Antibody quality control. RECOMMEND USAGE To prepare 1-10mg/ml carboxypeptidase B with sterile water or 25mM Tris-HCl pH 7.5. The ratio to aimed protein is 1:500 to 1:1000 (w/w), the optimum pH is pH7-9. STORAGE AND STABILITY Recommend recombinant carboxypeptidase B lyophilized powder stored under 2-8℃ in sealed container. It is stable within 24 months. After dissolved, it should be stored under -20℃, It is stable within 24 months and no activity lose after 10 times repeated freezing and thawing. RELATED PRODUCT: Recombinant Trypsin (sequencing purity), Recombinant Carboxypeptidase B (sequencing purity), V8 (sequencing purity), Recombinant Chymotrypsin (sequencing purity)