SG-Chymotrypsin™ (2 Citations)
SG-Chymotrypsin™ is a serine endopeptidase, which predominantly cleaves peptide bonds on the carboxy side of tyrosine, phenylalanine and tryptophan. In addition, chymotrypsin has a low catalytic activity against the carboxy side of leucine, methionine, alanine, aspartic and glutamic acids. It is therefore recommended to always use the shortest digestion time possible.
SG-Chymotrypsin™ is first treated with TLCK to inhibit trypsin that may be present and then subjected to an extensive purification process to remove contaminating protease and chymotryptic autolysis by-products. The highly purified enzyme is then chemically modified to increase its resistance to autolysis and stability.
For protein digestion 5ng/µl SG-Chymotrypsin is typically added to the protein at a ratio of 1:20 to 1:100 enzyme to protein, by weight in a standard digestion buffer. Incubate at 37°C for 2 to 10 hours, but can be extended to 24 hours, due to the extended life of the SG-Chymotrypsin™. We recommend choosing a ratio of enzyme to protein that allows for the shortest incubation time possible. This will reduce or eliminate the catalyzed hydrolysis of peptide bonds with non-aromatic amino acid residues.
- Modified Chymotrypsin 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.
|Material Safety Data Sheet|
|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|