SG-Arginine-C™ endopeptidase (Clostripain, from C. histolyticum) specifically hydrolyzes the carboxy peptide bond of Arginine. SG-Arginine-C™ has been modified chemically by a propriety process to render the enzyme resistant to autolysis and stabilize enzymatic activity. In addition, as a sulfhydryl enzyme, SG-Arginine-C™ is susceptible to inactivation by oxidation and as a result requires reducing agents for protection. The enzyme also requires calcium ion for maximal activity. A special reconstitution buffer is supplied, which contains reducing agents and activators to maintain enzyme activity.
SG-Arginine-C™ is supplied lyophilized in an activated form in 10μg vials and can be reconstituted to a concentration of 5ng/μl. For fragmentation the enzyme is added to the sample protein in a ratio of 1:10 to 1:20 (enzyme to protein, by weight)
- Modified Arginine-C for sequence analysis.
- Resistant to autolysis and degradation.
- High Specificity, free from other known endopeptidases.
- Consistency of activity levels from lot to lot for reproducible digestions.
- Digestion of proteins for sequence analysis.
- Suitable for sequencing applications.