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324714 Endoproteinase Lys-C, Lysobacter enzymogenes

324714
  
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Overview

Replacement Information
Description
Overview

This product has been discontinued.



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.

Catalogue Number324714
Brand Family Calbiochem®
References
ReferencesJekel, P.A., et al. 1983. Anal. Biochem. 134, 347.
Product Information
CAS number72561-05-8
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol of Tos-Gly-Pro-Lys-<i>p</i>NA per min at 25°C, pH 7.7.
EC number3.4.21.50
FormLyophilized
Quality LevelMQ100
Applications
Biological Information
Specific Activity≥150 units/mg protein
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
R PhraseR: 20-36/37/38-42/43

Harmful by inhalation.
Irritating to eyes, respiratory system and skin.
May cause sensitization by inhalation and skin contact.
S PhraseS: 22-26-36

Do not breathe dust.
In case of contact with eyes, rinse immediately with plenty of water and seek medical advice.
Wear suitable protective clothing.
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Harmful
Storage +2°C to +8°C
Do not freeze Ok to freeze
Special InstructionsFollowing 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.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
324714 0

Documentation

Endoproteinase Lys-C, Lysobacter enzymogenes MSDS

Title

Safety Data Sheet (SDS) 

Endoproteinase Lys-C, Lysobacter enzymogenes Certificates of Analysis

TitleLot Number
324714

References

Reference overview
Jekel, P.A., et al. 1983. Anal. Biochem. 134, 347.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision19-June-2008 RFH
DescriptionNative 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.
FormLyophilized
Recommended reaction conditions
Protocol Method 1: 1. Add the endoproteinase to the substrate at a concentration of 1:100 (protease:protein by weight) in 100 mM ammonium bicarbonate, pH 9.0. 2. Incubate for 1-2 h at 37°C. 3. Add a second aliquot or protease equal to the initial amount added and continue to incubate at 37°C for 11 h. Method 2: 1. Alternatively, mix the endoproteinase with the substrate at a concentration of 1:100 by weight in 100 mM ammonium bicarbonate, pH 8.5, containing SDS (1 mg/ml). 2. Incubate for 2 h at 37°C. 3. Add a second aliquot of protease equal to the initial amount added and incubate at 37°C. 4. Remove aliquots at timed intervals and monitor the progress of the digestion by electrophoresis.
CAS number72561-05-8
EC number3.4.21.50
Specific activity≥150 units/mg protein
Unit definitionOne 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.
SolubilityH₂O
Storage +2°C to +8°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing 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.
Toxicity Harmful
ReferencesJekel, P.A., et al. 1983. Anal. Biochem. 134, 347.