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525200 Phospholipase D, Streptomyces chromofuscus

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525200
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525200-250U
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      Description
      OverviewNative phospholipase D from Streptomyces chromofuscus. Catalyzes the hydrolysis of lecithin to phosphatidic acid and choline. Coupled with choline oxidase, it can also be used for the determination of phospholipids in serum.
      Catalogue Number525200
      Brand Family Calbiochem®
      SynonymsPLD
      References
      ReferencesKurz, T., et al. 1993. Circ. Res. 72, 701.
      Natarajan, V., and Garcia, J.G. 1993. J. Lab. Clin. Med. 121, 337.
      Yamamoto, I., et al. 1993. Biochim. Biophys. Acta 1145, 293.
      Product Information
      CAS number9001-87-0
      Activity≥50 units/mg dry weight
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmol of phosphatidylcholine per min at 37°C, pH 8.0.
      EC number3.1.4.4
      FormLyophilized brownish solid
      Quality LevelMQ100
      Applications
      Biological Information
      Physicochemical Information
      ContaminantsAatalase, glucose oxidase: none detected
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      R PhraseR: 20/21/22

      Harmful by inhalation, in contact with skin and if swallowed.
      S PhraseS: 36

      Wear suitable protective clothing.
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Harmful
      Storage -20°C
      Protect from Moisture Protect from moisture
      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 6 months at 4°C or for up to 1 year at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Número de referencia GTIN
      525200-250U 04055977270631

      Documentation

      Phospholipase D, Streptomyces chromofuscus Ficha datos de seguridad (MSDS)

      Título

      Ficha técnica de seguridad del material (MSDS) 

      Phospholipase D, Streptomyces chromofuscus Certificados de análisis

      CargoNúmero de lote
      525200

      Referencias bibliográficas

      Visión general referencias
      Kurz, T., et al. 1993. Circ. Res. 72, 701.
      Natarajan, V., and Garcia, J.G. 1993. J. Lab. Clin. Med. 121, 337.
      Yamamoto, I., et al. 1993. Biochim. Biophys. Acta 1145, 293.
      Ficha técnica

      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.

      Revision26-August-2008 RFH
      SynonymsPLD
      DescriptionNative phospholipase D from Streptomyces chromofuscus. Catalyzes the hydrolysis of lecithin to phosphatidic acid and choline; coupled with choline oxidase, it can be used for the determination of phospholipids in serum.
      FormLyophilized brownish solid
      CAS number9001-87-0
      EC number3.1.4.4
      ContaminantsAatalase, glucose oxidase: none detected
      Activity≥50 units/mg dry weight
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmol of phosphatidylcholine per min at 37°C, pH 8.0.
      Solubility10 mM Tris-HCl, pH 8.0, 0.05% BSA, and 0.1% (w/v) TRITON® X-100 (1 mg/ml)
      Storage Protect from moisture
      -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 6 months at 4°C or for up to 1 year at -20°C.
      Toxicity Harmful
      ReferencesKurz, T., et al. 1993. Circ. Res. 72, 701.
      Natarajan, V., and Garcia, J.G. 1993. J. Lab. Clin. Med. 121, 337.
      Yamamoto, I., et al. 1993. Biochim. Biophys. Acta 1145, 293.