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.
Unit Definition
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.
Reconstitution
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.
signalword
Danger
hcodes
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service