| SG-Arginine-C? endopeptidase (Clostripain, from C. histolyticum) specifically hydrolyzes the carboxy peptide bond of Arginine and 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 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 protein sample in a ratio of 1:100 to 1:20 (enzyme to protein, by weight). Features: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. Recommended SG-Arginine-C? to protein ratio, 1:100 to 1:20. Application for digestion of proteins for sequence analysis and suitable for sequencing applications. |
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