Trypsin Protease, 15000u, Mass Spectrometry Grade

Trypsin specifically hydrolyzes peptide bonds at the C-terminus of lysine and arginine residues. Unmodified trypsin is subject to residues generated by the autolysis of the protease, affecting HPLC peptide analysis. Furthermore, autolysis can lead to pseudotrypsin products, exhibiting characteristics of chymotrypsin. Mass spectrometry-grade trypsin is a modified porcine trypsin, which prevents protein hydrolysis through reductive methylation. Mass spectrometry-grade modified trypsin was further improved by TPCK treatment and affinity purification to generate highly active and stable molecules.

Physical Form: Mass spectrometry-grade trypsin protease is provided as a lyophilized powder.
Reconstitution Solution: Trypsin protease reconstitution buffer — recommended to use 1 mM HCl.
Shelf Life: 12 months when stored at -20°C.
pH Range: Shows maximum activity between pH 7–9; completely inactive at pH 4.
Application: Trypsin protease specifically hydrolyzes denatured proteins at lysine (K) and arginine (R) residues. Co-digestion with rLys-C is recommended.
Recommended SOP: General solution digestion method.
Use trypsin protease at a protein-to-enzyme ratio of 25–100:1 (w/w), incubate at 37°C for 5–12 hours overnight.

Cleavage Sites: R, K

Please contact us at for specific academic pricing.

More Details