General Description
Arginine-C is a sulfhydryl proteinase associated with collagenase and isolated from Clostridium histolyticum. Arginine-C endopeptidase (Clostripain, from C. histolyticum) specifically hydrolyzes the carboxy peptide bond of Arginine. In addition, as a sulfhydryl enzyme, Arginine-C is susceptible to inactivation by oxidation and as a result requires reducing agents for protection.
Our Arginine-C is highly purified and suitable in proteomics work for peptide mapping and protein sequence work due to its highly specific cleavage of peptides resulting in a limited number of fragments.
Features:
- Cleaves at the C-terminus of arginine residues, including sites next to proline
- Also cleaves at lysine residues
- Activity is optimal in the pH range of 7.6–7.9
Applications:
- Digestion of proteins for sequence analysis.
- Suitable for sequencing applications.
