General description
Native endoproteinase Lys-C from Lysobacter enzymogenes. Serine protease that specifically hydrolyzes amide or ester bonds at the carboxylic side of lysine in peptides and proteins. Useful for sequence and structural analysis. Inhibited by aprotinin, DFP, leupeptin, and TLCK. Has an optimal pH of 8.5-8.8.
Preparation Note
Following reconstitution, aliquot and freeze (-20°C) for long term storage or refrigerate (4°C) for short term storage. Stock solutions are stable for up to 2 days at 4°C or for up to 1 month at -20°C.
Other Notes
One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmol of Tos-Gly-Pro-Lys-pNA per min at 25°C, pH 7.7.
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P A Jekel et al.
Analytical biochemistry, 134(2), 347-354 (1983-10-15)
Endoproteinase Lys-C from Lysobacter enzymogenes, which is commercially available, proved to be useful in the determination of primary structures of proteins. The enzyme preferentially cleaves at the carboxyl side of lysine residues.
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