Lys-C Protease

Lys-C Protease, also called endoproteinase Lys-C, is a serine protease enzyme that hydrolyzes at C-terminal lysines and is often used in protein cleavage applications. First isolated from the bacterium Lysobacter enzymogenes, it has a molecular weight of 30 kDa. It is highly specific for lysine residues, including those followed by prolines. In comparison with trypsin, which cleaves after lysines and arginines, Lys-C generates peptide fragments that are longer and with less complexity. Trypsin/Lys-C mixes, which combine both enzymes, receive the benefits of both. Lys-C shows optimal activity at a pH range of 7.0 to 9.0 and remains active even under strong denaturing conditions. Mass spectrometry grade Lys-C is used for protein digestion, phosphopeptide enrichment workflows, peptide mass fingerprinting, and in-solution or in-gel digestion to produce peptides for LC-MS/MS protein identification. Visit the supplier page for more enzyme information.