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324796 Endopeptidase Lys-C, Achromobacter lyticus

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324796
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      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
      Quality LevelMQ100
      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
      324796-2U 04061838437662

      Documentation

      Endopeptidase Lys-C, Achromobacter lyticus SDS

      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.