ARG-C PROTEASE, 2X5UG

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 of5ng/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) 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. Applications Digestion of proteins for sequence analysis. Suitable for sequencing applications.