Description
Arg-C is a sulfhydryl cysteine protease (endopeptidase), isolated from Clostridium histolyticum and is also known as Clostripain. Arg-C specifically cleaves peptide, ester, and amide bonds at the C-terminal side of arginine residues. The specificity of Arg-C is primarily to arginine residues, but a minor degree of hydrolysis also takes place in most lysine-containing substrates. Reducing agents, such as DTT and Ca2+ are required for full its activity. In addition, as a sulfhydryl enzyme, Arg-C is susceptible to inactivation by oxidation and as a result requires reducing agents for protection. Our Arg-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:
- Specific cleavage of proteins and peptides for peptide mapping, fingerprinting, and sequence analysis
- digest proteins in solution, in gels, or on blotting membranes
Additional information
| Size | 1 x 10 µg, 2 x 10 µg |
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