Trypsin is a serine protease that specifically cleaves at the carboxylic side of lysine and arginine residues. The stringent specificity of trypsin is essential for protein identification.
- Lysine residues modified by reductive methylation, yielding a highly active and stable trypsin
- Frozen
The specificity of the purified trypsin is further improved by TPCK treatment, which inactivates chymotrypsin. The treated trypsin is then purified by affinity chromatography and lyophilized.
It is resistant to mild denaturing conditions such as 0,1% SDS, 1 M urea or 10% acetonitrile and retains 50% of its activity in 2 M guanidine HCl. The activity of trypsin is decreased when acidic residues are present on either side of a susceptible bond. If proline is at the carboxylic side of lysine or arginine, the bond is almost completely resistant to cleavage.
Reaction buffer: 50 mM NH4HCO3 (pH 7,8).
Delivery information: Kit includes Sequencing grade modified trypsin, porcine, frozen and trypsin resuspension dilution buffer.
