Trypsin, the most widely used protease in mass spectrometry analysis, utilizes its high specificity to cleave proteins, resulting in peptides with a strong C-terminal charge. When working with tightly folded proteins, these proteins can resist trypsin digestion and inadequate distribution of trypsin cleavage sites in certain proteins can generate peptides that are either too long or too short. In addition, post-translation modification (PTMs) present yet another challenge because glycans often limit trypsin access to cleavage sites, whereas acetylation or di- and trimethylation of lysine and arginine residues make them resistant to trypsin digestion. Promega offers several alternative proteases and a unique surfactant that can complement standard tryptic digestions to provide enhanced data.
Increase Protein Sequence Coverage With:
Enhance Digestion of Difficult Proteins With:
Improve Data for PTM Analysis With: