Engineered Specificity for Reliable Tag Removal
RECOMBINANT ENTEROKINASE
Scientific Background
- Specific cleavage after the sequence Asp-Asp-Asp-Asp-Lys↓
- Recombinant expression in yeast ensures animal-free production
- High purity and batch-to-batch consistency for reliable performance
- Minimal non-specific cleavage, ideal for fusion protein tag removal
- Essential in bioprocessing for protein activation and purification workflows
application
- Removes affinity tags (His-, GST-, MBP-) with high precision.
- Enables activation or maturation of therapeutic proteins.
- Supports controlled proteolysis for structure–function studies.
- Used in production of diagnostic reagents requiring specific cleavage.
- Ideal for GMP-grade, animal component–free bioprocessing.
Carboxypeptidase B
Scientific Background
- Carboxypeptidase B (CPB) (CAS Number 9025-24-5) is an enzyme that play a crucial role in the field of protein analysis, specifically in the precise determination of protein sequences and post-translational modifications
- CPB is Zn** metalloprotease that hydrolyses basic amino acids L-Lys and L-Arg from the C-terminal position in polypeptides
- CPB consists of 307 amino acids with a molecular weight of 34.5 kDa and pl 5.76
- Recombinant CPB derived from recombinant DNA technology, offers enhanced performance, reliability, regulatory compliance and versatility for a wide range of biopharma applications
Applications
- Peptide mapping and protein sequencing
- Determination of protein C-terminal amino acid
- Sequence analysis by successive cleavage of C-terminal basic amino baso animoacids
- Therapeutic insulin production by converting pro-insulin to insulin
- Therapeutic monoclonal antibodies manufacturing and quality control C Pep