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| Product Name | Recombinant Carboxypeptidase B, Animal-Free Lyophilised Powder (at least 170 USP U/mg) |
| Catalog No. | IVDRM-0295 |
| Description | Carboxypeptidase B trims basic residues from the C-terminus of a polypeptide, releasing lysine, arginine and histidine from the carboxyl end. Because that activity is needed in preparing recombinant insulin and other peptides, supply often depends on pancreas-derived material with the viral and consistency questions that brings. This enzyme is produced in Escherichia coli, free of any animal-derived component, and its amino acid sequence is identical to that of the rat pancreatic enzyme, so the kinetics are unchanged: an optimum between pH 7.5 and 9.0 and an isoelectric point near 6.0. The lyophilised powder is specified at not less than 170 USP units per milligram of protein and shows a single band on SDS-PAGE with no other proteolytic activity. |
| Intended Use | Removal of C-terminal basic residues during recombinant peptide manufacture and general biotechnology processes that need a defined exopeptidase. |
| Principle / Technology | The exopeptidase hydrolyses the peptide bond on the amino side of terminal lysine, arginine or histidine residues, shortening the chain one residue at a time from the carboxyl end. |
| Sample Type | Peptide intermediates and recombinant protein preparations in solution. |
| Performance Range / Specifications | Activity not below 170 USP units per milligram of protein; single band on SDS-PAGE with no other protease; animal-free production; matches the kinetics of animal-derived carboxypeptidase B with an optimum of pH 7.5 to 9.0 and an isoelectric point of 6.0. |
| Specificity | Theoretical molecular weight 33.8 plus or minus 3.4 kDa; activity at least 170 USP units per milligram of protein; optimum pH 7.5 to 9.0; isoelectric point 6.0; produced under GMP rules; supplied as 1 mg, 10 mg, 100 mg or 1 g of powder. |
| Reaction Conditions / Protocol | Dissolve the powder in a buffer matched to the process pH, add it to the peptide solution at the calculated ratio, incubate at around 25 °C, then monitor the disappearance of the extended intermediate by chromatography. |
| Components / Formulation | Lyophilised enzyme powder, one vial per ordered quantity. |
| Storage Conditions | Keep the dry powder at 2 to 8 °C; hold reconstituted solution at -25 to -15 °C. |
| Shelf Life | 2 years for the powder; reconstituted solution survives repeated freezing without activity loss. |
| Package Specifications | Supplied as 1 mg, 10 mg, 100 mg or 1 g of lyophilised powder. |
| Product Form | White, off-white or slightly yellow lyophilised powder. |
| Quality Control | Released against specific activity, single-band appearance by SDS-PAGE and absence of other proteolytic activity. |
| Key Features | - Sequence identical to the rat pancreatic enzyme with no animal-derived input - Specific activity at least 170 USP units per milligram - Single band on SDS-PAGE with no contaminating protease - Produced under GMP rules for process use - Reconstituted solution tolerates repeated freeze-thaw cycling |
| Purity | A single clear target band is seen by SDS-PAGE with no contaminating protease activity. |
| Concentration | Specific activity not below 170 USP units per milligram of protein. |
| Activity / Unit Definition | One unit catalyses the hydrolysis of one micromole of hippuryl-L-arginine per minute at 25 °C and pH 7.6. |
| Molecular Weight | 33.8 plus or minus 3.4 kDa theoretical. |
| Source / Origin | Recombinant expression in Escherichia coli; no animal-derived components in production. |
| pH Range / Optimal pH | Optimum between pH 7.5 and 9.0; isoelectric point 6.0. |
| Shipping Conditions | Shipped cold. |
| Expiration Date / Stability | Reconstituted enzyme withstands ten freeze-thaw cycles without measurable activity loss. |
| Regulatory / Compliance | Supplied for laboratory research purposes. |
| Compatibility | Usable wherever animal-derived carboxypeptidase B would be applied in bioprocessing. |
| Recommended Buffer System | Reconstitute in a buffer near the optimum pH range for the intended reaction. |
| Application Notes / Precautions | Activity falls in the presence of chelators such as EDTA and is competitively inhibited by free arginine and lysine, so high concentrations of those residues slow the reaction. |
| Batch-to-Batch Consistency | Each production lot is released against fixed acceptance criteria so performance stays consistent between orders. |
| Model Type | C-terminal processing exopeptidase |
| Starting Material / Tissue Site | Recombinant enzyme from Escherichia coli matching the rat pancreatic sequence |
| Delivery Standard | Vial of lyophilised powder |
| Turnaround Time | No lead time is published on the product page; availability is confirmed when the order is placed. |
| Readouts / Downstream Assays | Disappearance of the extended intermediate and appearance of the trimmed product followed by chromatography or mass analysis. |
For in vitro diagnostic use.
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