Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Unmodified trypsin is prone to autolysis, generating fragments that can interfere with protein sequencing or HPLC peptide analysis. Furthermore, autolysis can result in the generation of pseudotrypsin, which exhibits chymotrypsin-like specificity. Mass Spec Grade modified trypsin is porcine trypsin modified by reductive methylation, rendering it resistant to autolytic digestion. Enzymatic stability tests demonstrate that modified trypsin does not self-hydrolyze and retains higher activity compared to general trypsin.
Physical Appearance
Lyophilized powder
Molecular Weight
23 kDa
Resuspension Buffer
Trypsin Resuspension Buffer is composed of 1 mM hydrochloric acid.
Storage
Store the lyophilized powder at –20 °C; store reconstituted enzyme at –80 °C.
Shelf life
24 months at -20 ℃
Stability
Modified trypsin is maximally active in the pH range of 7–9 and reversibly inactivated at pH 4.
Usage Notes
For maximum activity, resuspend trypsin in the provided resuspension buffer and heat at 30 °C for 15 min before use. Thaw the reconstituted trypsin at room temperature, placing on ice immediately after thawing. Add trypsin at a protease:protein ratio in the range of 1:100 - 1:25 (w/w) for protein identification (recommended). Mix well and incubate at 37 °C for 4 h.
Download Datasheet
For Research or Industrial Raw Materials, Not For Personal Medical Use!