Science & Applications

LysN cleaves on the N-terminal side of lysine (↓K) while trypsin cleaves on the C-terminal side of lysine and arginine (K/R↓). This generates completely different peptide sets with complementary sequence coverage.

LysN doesn't express well in recombinant systems, requiring purification from natural sources (mushrooms). This makes production more challenging than recombinant enzymes like trypsin. We've developed proprietary purification methods to ensure consistent supply.

Yes, LysN can be used as an alternative to trypsin for many proteomics applications. It's particularly valuable for DIA proteomics and when you need different peptide coverage. Many researchers use both enzymes for comprehensive protein characterization.

LysN-generated peptides have greater spread in the ion mobility dimension compared to tryptic peptides. This reduces peak overlap and co-elution, improving peptide identification confidence in complex samples.

We recommend 1:50 to 1:100 (w/w) enzyme:substrate ratio. Start with 1:50 for difficult proteins and 1:100 for routine digestions. Overnight incubation (16 hours) at 37°C typically provides complete digestion.

Compatible with isobaric and metabolic labeling strategies (e.g., TMT®, iTRAQ®, Stable isotope labeling of cells in culture (SILAC)).