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: Recombinant Carboxypeptidase B Animal Origin Free, No Virus Contaminant 1-Recombinant Carboxypeptidase B.rar 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 (EC 3.4.17.2) 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. ADVANTAGES Animal origin free YaxinBio recombinant carboxypeptidase B belongs to the AOF level 3. Level 3 recombinant carboxypeptidases B eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B. Stable A sterile recombinant carboxypeptidase B lyophilized powder eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. It is also very convenient for transport and storage. High purity 1) Recombinant carboxypeptidase B provides increased specificity and eliminates contaminating activities found in enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. Less than 10ppm of recombinant trypsin. 3) One single main band at 35kD by SDS-PAGE. Figure 1. SDS-PAGE of YaxinBio Recombinant Carboxypeptidase B (RCPB) MAIN FEATURES Source E.Coli Purified by HPLC Physical form White or white-like lyophilized powder Additives Tris salts, NaCl salts and carbohydrates. Protein content 35% ～ 50% Specific activity ≥120 units/mg pro.;≥170 units/mg pro. Purity ≥95% Contaminant activity No chymotrypsin, carboxypeptidase A, and other protease contaminant. Less than 10ppm band at 35kD by SDS-PAGE.