SG-Chymotrypsin™

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.

Features

• 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.

Applications

• Digestion of proteins for sequence analysis.

• Suitable for sequencing applications.