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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.
Catalogue Number
324715
Brand Family
Calbiochem®
References
References
Jekel, P.A., et al. 1983. Anal. Biochem. 134, 347.
Product Information
CAS number
72561-05-8
Unit of Definition
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol Tos-Gly-Pro-Lys-<i>p</i>NA per min at 25°C, pH 7.7.
EC number
3.4.21.50
Form
Lyophilized
Formulation
Lyophilized from 50 mM HEPES, 10 mM EDTA, 5 mg/ml raffinose, pH 8.0.
Harmful by inhalation. Irritating to eyes, respiratory system and skin. May cause sensitization by inhalation and skin contact.
S Phrase
S: 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
Hygroscopic
Hygroscopic
Do not freeze
Ok to freeze
Special Instructions
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.
Jekel, P.A., et al. 1983. Anal. Biochem. 134, 347.
数据表
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.
Revision
01-February-2012 RFH
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.
Form
Lyophilized
Formulation
Lyophilized from 50 mM HEPES, 10 mM EDTA, 5 mg/ml raffinose, pH 8.0.
Recommended reaction conditions
Protocol
1. Dissolve the proteins to be sequenced in 25 mM Tris-HCl, pH 8.5, and 1 mM EDTA. For proteins that are difficult to solubilize, add urea, SDS, or guanidine-HCl to the digestion buffer prior to solubilization. If urea is used, add 20 mmol/l of methylamine.
2. The suggested working concentration is 1:20-1:100 (protease:protein by weight).
3. Incubate for 2-18 h at 37°C.
CAS number
72561-05-8
EC number
3.4.21.50
Purity
≥90% by SDS-PAGE
Specific activity
≥200 units/mg protein
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.
Solubility
Reconstitute in 50 µl of distilled H₂O.
Storage
+2°C to +8°C
Hygroscopic
Do Not Freeze
Ok to freeze
Special Instructions
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.
Toxicity
Harmful
References
Jekel, P.A., et al. 1983. Anal. Biochem. 134, 347.
