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324796 Endopeptidase Lys-C, Achromobacter lyticus

Endopeptidase Lys-C, Achromobacter lyticus MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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324796
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
324796-2UCN 玻璃瓶 2 u
Description
OverviewNative endopeptidase Lys-C from Achromobacter lyticus. Lysyl endopeptidase is a serine protease secreted by soil bacteria and specifically hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues.
Catalogue Number324796
Brand Family Calbiochem®
References
ReferencesJekel, P.A., et al. 1983. Anal. Biochem. 134, 347.
Product Information
CAS number78642-25-8
Unit of DefinitionOne AU (amidase unit) is defined as the amount of enzyme that catalyzes the release of 1 µM <i>p</i>NA from <i>N</i>-benzoyl-DL-lysine-<i>p</i>NA per min at 30°C, pH 9.5.
FormLyophilized
HS Code3507 90 49
Quality SegmentMQ100
Applications
Biological Information
Specific Activity≥2 AU/mg protein
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Blue Ice Only
Toxicity Standard Handling
Storage -20°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 year at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade ITEM Number
Catalogue Number GTIN
324796-2UCN 04061838437662

Documentation

Endopeptidase Lys-C, Achromobacter lyticus MSDS

Title

Safety Data Sheet (SDS) 

Endopeptidase Lys-C, Achromobacter lyticus Certificates of Analysis

TitleLot Number
324796

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 endopeptidase Lys-C from Achromobacter lyticus. Lysyl endopeptidase is a serine protease secreted by soil bacteria and specifically hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues. Optimal pH: 9.0-9.5.
FormLyophilized
Recommended reaction conditionsAmidase Activity: Materials Required: •Reagent A: 200 mM AMP, pH 9.5 (dissolve 4.2 g 2-amino-2-methyl-1,3-propanediol in 150 ml H2O; adjust the pH to 9.5 with 1 M HCl; add H2O to a final volume of 200 ml) •Reagent B: 2.5 mM Bz-Lys-pNA (dissolve 22.6 mg Nα-benzoyl-DL-lysine-p-nitroanilide in 900 ml H2O) •Reagent C: enzyme diluent (dissolve 240 µg 2-amino-2-hydroxymethyl-1,3-propanediol in 900 ml H2O; adjust the pH to 8.0 with 0.1 M HCl; add H2O to a final volume of 1 L •Reagent D: enzyme solution (dissolve 1 vial enzyme in 1 ml H2O; dilute 100 µl to a final volume of 25 ml with Reagent C) •45% Acetic Acid (stop solution) Protocol 1. Add 2.6 ml Reagent A to 300 µl Reagent B and pre-incubate at 30°C to equilibrate the temperature. 2. Add 100 µl Reagent D and incubate for 25 min at 30°C. Include 100 µl Reagent C alone as a control. 3. Add 1 ml 45% acetic acid to stop the reaction. 4. Measure the absorbance at 405 nm. 5. Calculate the activity: Amidase Activity (AU/vial) = [(Atest-Acontrol)/25] x [1/9.62] x [4/0.1] x 250
CAS number78642-25-8
Specific activity≥2 AU/mg protein
Unit definitionOne AU (amidase unit) is defined as the amount of enzyme that catalyzes the release of 1 µM pNA from N-benzoyl-DL-lysine-pNA per min at 30°C, pH 9.5.
SolubilityH₂O or Tris-HCl buffer, pH 4-11. Reconstitute 1 vial with 1 ml solvent; if the enzyme is not completely solubilized, add 1-3 ml additional solvent until completely dissolved.
Storage Avoid freeze/thaw
-20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 1 year at -20°C.
Toxicity Standard Handling
ReferencesJekel, P.A., et al. 1983. Anal. Biochem. 134, 347.