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217372 Carboxypeptidase Y, Excision Grade, Yeast

217372
  
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      Replacement Information

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      Description
      Overview

      This product has been discontinued.



      We apologize for the inconvenience, but we do not currently have an alternative product.






      Native carboxypeptidase y from yeast. Serine protease that specifically cleaves C-terminal amino acids from proteins, with a preference for hydrophobic amino acids. Hydrolysis of C-terminal aspartic acid or glycine is very slow. Designed for the determination of C-terminal residues during protein sequencing.
      Catalogue Number217372
      Brand Family Calbiochem®
      References
      ReferencesStennicke, H.R., et al. 1994. Protein Eng. 7, 911.
      Product Information
      CAS number9046-67-7
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Ala from z-Phe-Ala per min at 37°C, pH 6.0.
      EC number3.4.16.1
      FormLyophilized
      FormulationLyophilized from 50 mM sodium citrate, pH 6.0.
      PI3.6
      Applications
      Biological Information
      Purity≥90% by SDS-PAGE
      Specific Activity≥300 units/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 Ambient Temperature Only
      Toxicity Standard Handling
      Storage -20°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 1 week at 4°C or for up to 1 month at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Carboxypeptidase Y, Excision Grade, Yeast Certificates of Analysis

      TitleLot Number
      217372

      References

      Přehled odkazů
      Stennicke, H.R., et al. 1994. Protein Eng. 7, 911.
      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.

      Revision03-June-2008 RFH
      DescriptionNative carboxypeptidase y from yeast. Serine protease that specifically cleaves C-terminal amino acids from proteins, with a preference for hydrophobic amino acids. Hydrolysis of C-terminal aspartic acid or glycine is very slow. Designed for the determination of C-terminal residues during protein sequencing.
      FormLyophilized
      FormulationLyophilized from 50 mM sodium citrate, pH 6.0.
      Recommended reaction conditions1:100 (protease:protein by weight) for sequence analysis. Has an optimal pH of 5.5-6.5 and a pI of 3.6.
      CAS number9046-67-7
      EC number3.4.16.1
      Purity≥90% by SDS-PAGE
      Specific activity≥300 units/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Ala from z-Phe-Ala per min at 37°C, pH 6.0.
      SolubilityReconstitute in 50 µl of distilled H₂O.
      Storage -20°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 1 week at 4°C or for up to 1 month at -20°C.
      Toxicity Standard Handling
      ReferencesStennicke, H.R., et al. 1994. Protein Eng. 7, 911.

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      Kategorie

      Life Science Research > Proteins and Enzymes > Other Enzymes