Carboxypeptidase B (EC 126.96.36.199) is exclusively used for the hydrolysis of protein C-terminal basic amino acids (lysine, arginine, histidine); also known as peptidyl-L-lysine (L -Arginine) hydrolase; sperminase. The molecular weight is 35kD, the isoelectric point is 6.0, and the optimum pH is 7-9. The activity is competitively inhibited by arginine and lysine, and metal ion chelating agents such as EDTA inhibit enzyme activity.
No animal origin: recombinant production, no foreign virus contamination, such as swine flu virus, porcine parvovirus, etc.
High purity: no other miscellaneous enzyme activity: no other side reactions in the digestion reaction, high yield
High specific activity: no less than 120 u/mg pro.; no less than 170 u/mg pro.
Electrophoresis purity: SDS-PAGE electrophoresis identification, 95%
Stable: freeze-dried powder, easy to store and transport
Recombinant carboxypeptidase B is a product of non-animal origin AOF3 level
Production of recombinant insulin and its analogues
Determination of protein C-terminal amino acid
Production of other recombinant peptides
Enzymatic synthesis of some special compounds