Product 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 UCF.ME™ R ecombinant CP B 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
Applications
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. |
Components
Storage
Lyophilized powder can be stored a t 2 ~ 8℃ for two y ear s
Manuals
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