SG-Arginine-C™ endopeptidase (Clostripain, from C. histolyticum) specifically hydrolyses 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 stabilise 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.
- 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
SG-Arginine-C™ is supplied lyophilised in an activated form in 5 μg vials and can be reconstituted to a concentration of 0,25 μg/ml by addition of 20 μl per vial of the supplied reaction buffer. For fragmentation the enzyme is added to the sample protein in a ratio of 1:100 to 1:20 (enzyme to protein, by weight)