Arg-C, Sequencing Grade

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