Application: Protein structure and sequence analysis, such as hydrolyze basic amino acids lysine, arginine and histidine from the C-terminal of polypeptides.<br />Antibody quality control.
Carboxypeptidase B catalyzes the hydrolysis of polypeptide C-terminal lysine, arginine and histidine. The molecular weight is 34500 Daltons, the optimum pH is 8.0, and the pI is 6.0. Carboxypeptidase B is competitively inhibited by arginine and lysine. This enzyme is also inhibited by metal chelators such as EDTA. Recombinant carboxypeptidase B was expressed in Escherichia coli and purified by high pressure liquid chromatography. There was no trace of activity of other enzymes such as carboxypeptidase A and chymotrypsin. No protease inhibitors (such as PMSF) are used in the production process.
Specification
Size: 100 μg CAS #: 9025-24-5 Enzyme Commission #: 3.4.17.2 Molecular weight: 34.5 kDa Origin: Rat Source: E.coli Purified by: HPLC Physical form: Lyophilized powder Specific activity: ≥200 units/mg protein Unit definition: One Unit of carboxypeptidase B activity hydrolyzes one micromole of hippuryl-L-arginine per minute at 25°C, pH 7.65. Contaminant activity: No trypsin, chymotrypsin, carboxypeptidase A, or other protease contaminants. Storage: Store in a sealed container at 2 - 8°C. Once reconstituted, it should be aliquoted and stored at -20°C. The product is stable for 24 months with no detectable loss of enzymatic activity after 10 repeated freeze-and-thaw cycles. Intended use: For research only. Not intended for any human or animal diagnostic or therapeutic use.
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