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345806 β1,4-Galactosidase, Streptococcus pneumoniae, Recombinant, E. coli

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345806
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概要

Replacement Information

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カタログ番号 在庫状況包装 Qty/Pk 価格 数量
345806-50MIUCN
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      樹脂アンプル 50 miu
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      Description
      OverviewRecombinant, Streptococcus pneumoniae β1,4-Galactosidase expressed in E. coli. Catalyzes the hydrolysis of non-reducing terminal β1,4-linked galactose. This enzyme is not known to cleave substituted or branched galactose. Inhibited by fucose attached to penultimate sugar.
      Note: 1 mU = 1 milliunit.
      Catalogue Number345806
      Brand Family Calbiochem®
      Synonymsβ1,4-D-Galactoside Galactohydrolase
      References
      ReferencesKierman, U.A., et al. 2004. Proteomincs 4, 1825.
      Prime, S., et al. 1996. J. Chromatogr. A. 720, 263.
      Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.
      Product Information
      CAS number9031-11-2
      Activity≥1.5 units/ml
      Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol <i>p</i>-nitrophenol from <i>p</i>-nitrophenyl-β-D-galactopyranoside per min at 37°C, pH 5.0.
      EC number3.2.1.23
      FormLiquid
      FormulationIn 25 mM NaCl, 20 mM Tris-HCl, pH 7.5. Sterile solution.
      Quality LevelMQ200
      Applications
      Biological Information
      Specific Activity≥6 units/mg protein
      Physicochemical Information
      ContaminantsN-acetylglucosaminidase, α-galactosidase, α-mannosidase, neuraminidases, proteases: none detected. Recommended reaction buffer: 50 mM sodium phosphate buffer, pH 6.0
      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 +2°C to +8°C
      Do not freeze Yes
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      カタログ番号 GTIN
      345806-50MIUCN 04055977194081

      Documentation

      β1,4-Galactosidase, Streptococcus pneumoniae, Recombinant, E. coli (M)SDS

      タイトル

      英語版製品安全データシート((M)SDS) 

      β1,4-Galactosidase, Streptococcus pneumoniae, Recombinant, E. coli 試験成績書(CoA)

      タイトルロット番号
      345806

      参考資料

      参考資料の概要
      Kierman, U.A., et al. 2004. Proteomincs 4, 1825.
      Prime, S., et al. 1996. J. Chromatogr. A. 720, 263.
      Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.
      データシート

      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.

      Revision30-June-2008 RFH
      Synonymsβ1,4-D-Galactoside Galactohydrolase
      DescriptionRecombinant, Streptococcus pneumoniae β1,4-Galactosidase expressed in E. coli. Catalyzes the hydrolysis of non-reducing terminal β1,4-linked galactose. This enzyme is not known to cleave substituted or branched galactose. Inhibited by fucose attached to penultimate sugar.
      FormLiquid
      FormulationIn 25 mM NaCl, 20 mM Tris-HCl, pH 7.5. Sterile solution.
      Recommended reaction conditions50 mM sodium phosphate buffer, pH 6.0.
      CAS number9031-11-2
      EC number3.2.1.23
      ContaminantsN-acetylglucosaminidase, α-galactosidase, α-mannosidase, neuraminidases, proteases: none detected. Recommended reaction buffer: 50 mM sodium phosphate buffer, pH 6.0
      Specific activity≥6 units/mg protein
      Activity≥1.5 units/ml
      Unit definitionOne unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol p-nitrophenol from p-nitrophenyl-β-D-galactopyranoside per min at 37°C, pH 5.0.
      Storage +2°C to +8°C
      Do Not Freeze Yes
      Toxicity Standard Handling
      ReferencesKierman, U.A., et al. 2004. Proteomincs 4, 1825.
      Prime, S., et al. 1996. J. Chromatogr. A. 720, 263.
      Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.