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567704 Sphingolipid Ceramide N-Deacylase, Pseudomonas sp.

SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.

Synonyme: SCDase

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567704
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Übersicht

Replacement Information

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567704-250MIU
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      Description
      OverviewNative sphingolipid ceramide N-deacylase from Pseudomonas species. Hydrolyzes the N-acyl linkage between fatty acids and the sphingosine base of ceramide in various sphingolipids and gangliosides. This enzyme can also catalyze the reverse reaction and transacylation. It is not recommended for hydrolysis of ceramide. Note: 1MU = 1 milliunit.
      Note: 1 mU = 1 milliunit.
      Catalogue Number567704
      Brand Family Calbiochem®
      SynonymsSCDase
      References
      ReferencesMitsutake, S., et al. 1997. Anal. Biochem. 247, 52.
      Sueyoshi, N., et al. 1997. J. Lipid Res. 38, 1923.
      Ito, M., et al. 1995. J. Biol. Chem. 270, 24370.
      Product Information
      Activity≥1 unit/ml.
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmol of asialo-GM₁ per min at 37°C, pH 6.0.
      EC number3.5.1.-
      FormLiquid
      FormulationIn 50 mM sodium acetate buffer, 0.1% LUBROL® PX Detergent, pH 6.0.
      Quality LevelMQ100
      Applications
      Biological Information
      Physicochemical Information
      Contaminantsα- and β-N-acetylgalactosaminidase, α-fucosidase, α- and β-galactosidase, neuraminidases: none detected
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Dry Ice Only
      Toxicity Standard Handling
      Storage -20°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Bestellnummer GTIN
      567704-250MIU 04055977190793

      Documentation

      Sphingolipid Ceramide N-Deacylase, Pseudomonas sp. SDB

      Titel

      Sicherheitsdatenblatt (SDB) 

      Sphingolipid Ceramide N-Deacylase, Pseudomonas sp. Analysenzertifikate

      TitelChargennummer
      567704

      Literatur

      Übersicht
      Mitsutake, S., et al. 1997. Anal. Biochem. 247, 52.
      Sueyoshi, N., et al. 1997. J. Lipid Res. 38, 1923.
      Ito, M., et al. 1995. J. Biol. Chem. 270, 24370.

      Broschüre

      Titel
      Gangliosides Technical Bulletin
      Datenblatt

      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.

      Revision18-September-2007 RFH
      SynonymsSCDase
      DescriptionNative sphingolipid ceramide N-deacylase from Pseudomonas species. Hydrolyzes the N-acyl linkage between fatty acids and the sphingosine base of ceramide in various sphingolipids and gangliosides. This enzyme can also catalyze the reverse reaction and transacylation. It is not recommended for hydrolysis of ceramide. Note: 1MU = 1 milliunit.
      FormLiquid
      FormulationIn 50 mM sodium acetate buffer, 0.1% LUBROL® PX Detergent, pH 6.0.
      EC number3.5.1.-
      Contaminantsα- and β-N-acetylgalactosaminidase, α-fucosidase, α- and β-galactosidase, neuraminidases: none detected
      Activity≥1 unit/ml.
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmol of asialo-GM₁ per min at 37°C, pH 6.0.
      Storage Avoid freeze/thaw
      -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Toxicity Standard Handling
      ReferencesMitsutake, S., et al. 1997. Anal. Biochem. 247, 52.
      Sueyoshi, N., et al. 1997. J. Lipid Res. 38, 1923.
      Ito, M., et al. 1995. J. Biol. Chem. 270, 24370.