Description: Trypsin is a serine endopeptidase. It selectively cleaves peptide bonds C-terminal to lysine and arginine residues. Trypsin is treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inactivate any remaining chymotryptic activity. It is modified by acetylation of the e-amino groups of lysine residues to prevent autolysis. Modified Trypsin cleaves at Lys-Pro and Arg-Pro bonds at a much slower rate than other amino acid residues. Source: Isolated from bovine (Bos taurus) pancreas Reagents Supplied: Trypsin Reaction Buffer General notes: Trypsin is acetylated on multiple lysine residues. This protein appears as a single band on SDS-PAGE. This sequence is also available at www.neb.com Store frozen at -20°C for up to one week. A decrease in activity will occur if stored in solution. Use only freshly reconstituted protease for best results. Reconstitution: Trypsin should be reconstituted by the addition of 20- 200 µl of high purity water. Rapid autolysis is a function of enzyme concentration. More information can be found on the main product page.