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Sigma-Aldrich

Endoproteinase Lys-C, Sequencing Grade, Lysobacter enzymogenes

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Synonym(s):
Endoproteinase Lys-C, Sequencing Grade, Lysobacter enzymogenes
CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352202

grade

Proteomics Grade

Quality Level

Assay

≥90% (SDS-PAGE)

form

lyophilized

specific activity

≥200 units/mg protein

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)

shipped in

ambient

storage temp.

2-8°C

Related Categories

General description

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.

Warning

Toxicity: Harmful (C)

Unit Definition

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.

Physical form

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

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.
Reconstitute in 50 µl of distilled H₂O.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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S Zhang et al.
The Journal of biological chemistry, 271(52), 33575-33579 (1996-12-27)
While multiple G protein beta and gamma subunit isoforms have been identified, the implications of this potential diversity of betagamma heterodimers for signaling through betagamma-regulated effector pathways remains unclear. Furthermore the molecular mechanism(s) by which the betagamma complex modulates diverse

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