Description
Carboxypeptidase B, also known as peptidyl-L-lysine (L-lysine) hydrolase or pancreatic carboxypeptidase B, is a specialized enzyme that hydrolyzes the amino group at the C-terminus of basic amino acids in proteins (Lysine (Lys, K), Arginine (Arg, R), and Histidine (His, H)). It has a molecular weight of 33.8 kD and an isoelectric point of 6.0, with an optimal pH range of 7.5 to 9.0. The activity of carboxypeptidase B is subject to competitive inhibition by arginine and lysine, and is inhibited by metal ion chelators such as EDTA.
Yeasen Recombinant CPB is expressed in E.coli, produced under GMP regulations, free of any animal-derived components, and without the risk of viral contamination from animal sources. The amino acid sequence is identical to that of rat pancreatic carboxypeptidase B, possessing the same enzymatic properties as the animal-derived enzyme, and can be used as a substitute in various biotechnological processes.
Features
1.Strong specificity—A specialized enzyme that hydrolyzes the amino group at the C-terminus of basic amino acids in proteins (Lysine (Lys, K), Arginine (Arg, R), and Histidine (His, H))
2.High purity—Purity≥95%.
3.Animal free—Recombinantly produced, free from exogenous viral contamination, and no animal-derived materials are used in the production process.
Applications
1.Production of recombinant insulin and its analogs.
2.Determination of the C-terminal amino acids of proteins.
3.Removal of the C-terminal histidine tag from proteins.
4.Production of other recombinant polypeptide substances.
5.Enzymatic synthesis of certain special compounds.
Specifications
|
Source |
E.coli recombinant expression |
|
Molecular Weight |
Theoretical value 33.8±3.4 kDa |
|
Appearance |
White, off-white, or pale yellow powder |
|
Enzyme Concentration |
≥170 USP units/mg pro |
|
Unit Definition |
At 25℃, pH 7.6, the amount of enzyme that catalyzes 1 μmoL of hippuryl-L-arginine hydrolysis in 1 minute is defined as one unit of enzyme activity. |
|
Quality Assurance |
SDS-PAGE gel detection shows a clear single band of the target protein; no other proteases present, no non-specific cutting. |
Storage
Lyophilized powder can be stored at 2 ~ 8℃ for two years.