Enzymes Recombinant Carboxypeptidase B E.coli Digestion of Protein
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids
lysine, arginine and histidine from the C-terminal end of
polypeptides. The molecular weight is 33.8kD, the optimum pH 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
① Animal origin free: Recombinant carboxypeptidase B is no
exogenous virus contamination,and any animal origin material is not
used in the production process.
② Stable quality: Mass production can ensure stable and continuous
batch production.It is no difference between the batch and the
product quality is stable.
③ High purity: Higher specific activity.No other contaminating
proteases such as chymotrypsin and carboxypeptidase A.Host protein
residues is less than the limits of biological products.
④ Lyophilized powder: The product is lyophilized powder and is
convenient to store and transport.
⑤ Compliance with regulatory requirements: Production equipment and
production environment comply with relevant regulatory
requirements, and the production process is in full compliance with
NSF ISO 9001: 2008 quality system and GMP guidelines.
⑥ Complete quality documents: we can provide relevant regular
support files in according to customers’ requirement.
White or white-like or yellowish lyophilized
Tris salts, NaCl salts and carbohydrates
Single main band on SDS-PAGE
Less than 10 ppm of recombinant trypsin.
Unit Definition:One Unit of carboxypeptidase B activity hydrolyzes one micromole of
hippuryl-L-arginine per minute at 25℃, pH 7.65.
Sequencing grade trypsin
Recombinant human trypsin