Endoproteinase Lys-C, Sequencing Grade, Lysobacter enzymogenes

Native endoproteinase Lys-C from Lysobacter enzymogenes. Serine protease that specifically hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine in peptides and proteins. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Inhibited by aprotinin, DFP, leupeptin, and TLCK.

Native endoproteinase Lys-C from Lysobacter enzymogenes. Serine protease that specifically hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine in peptides and proteins. Designed for protein sequencing or sequence verification, analysis of protein structural domains, and cleavage of fusion proteins. Inhibited by aprotinin, DFP, leupeptin, and TLCK. Suggested working concentration: 1:20 to 1:100 (protease:protein by weight) for sequence analysis.

Toxicity: Harmful (C)

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Tos-Gly-Pro-Lys-pNA per min at 25°C, pH 7.7.

Lyophilized from 50 mM HEPES, 10 mM EDTA, 5 mg/ml raffinose, pH 8.0.

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.

Reconstitute in 50 µl of distilled H₂O.

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