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SG-Arginine-C™ (1 Citations)

 

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)

 


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.
Protocol
786-11
Material Safety Data Sheet
786-11
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Technical Literature
Mass Spectrometry Sample Prep Handbook A guide to the preparation of protein samples for Mass Spectrometry, including protein extraction, clean-up and peptide generation.
Protease & Phosphatase Inhibitors & Proteases Handbook  A handbook & selection guide for inhibitors of protease & phosphatases & for proteases & assays

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