1. Product Introduction
Recombinant Carboxypeptidase B 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.
2. Product advantages
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
Figure 1. Diagram of the production process of different levels of non-animal origin of biological products
Recombinant carboxypeptidase B is a product of non-animal origin AOF3 level
3. Product use
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
4. Product features
Source: Recombinant Escherichia coli
Product properties: white or almost white freeze-dried powder
Electrophoresis identification and Coomassie brilliant blue staining
12%SDS-PAGE: molecular weight 35kD, single main band
Specific activity: not less than 120 u/mg pro.; not less than 170 u/mg pro.
Other enzyme content: no chymotrypsin, carboxypeptidase A, etc., trypsin is not detected. Trypsin content is less than 10ppm
Does not contain any protease inhibitors: No protease inhibitors such as PMSF, EDTA, etc.
Figure 2. SDS-PAGE identification and purity analysis of recombinant carboxypeptidase B freeze-dried powder
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