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03-189 CBP (catalytic domain) human recombinant

CBP (catalytic domain) human recombinant protein expressed in E. Coli.

CBP (catalytic domain) human recombinant: Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.
Key Applications: Enzyme Assays UniProt Number: Q92793
03-189
100 µg  
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      Descripción

      Replacement Information

      Tabla espec. clave

      Key ApplicationsSpeciesUni Prot Number
      Enzyme AssaysHuman Q92793
      Description
      Catalogue Number03-189
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionCBP (catalytic domain) human recombinant
      OverviewCBP (catalytic domain) human recombinant expressed in E. Coli
      Background InformationAlthough originally termed histone acetyltransferases (HATs) for their lysine acetylation activity on histone N-terminal tails, p300 and its paralogue, CBP, have been shown to acetylate a variety of non-histone proteins including p53, DNA polymerase ß and nuclear import factors. p300/CBP acetylations play regulatory roles in transcription, DNA repair and replication, the cell cycle, p53 turnover, and nuclear import. In addition to functions which overlap with those of CBP, p300 has a number of unique functions, including a role in the induction of p21Waf1/Cip1 cell cycle inhibitor.
      References
      Product Information
      FormatPurified
      PresentationIn liquid containing 50 mM Tris/HCl, pH 8.0, 0.1 mM EDTA, 10% glycerol. Frozen solution.
      Quality LevelMQ100
      Applications
      ApplicationCBP (catalytic domain) human recombinant protein expressed in E. Coli.
      Key Applications
      • Enzyme Assays
      Application NotesAcetyltransferase assays
      Biological Information
      PurityPurity >65% by SDS-PAGE
      SourceCatalytic domain (residues 1319-1710) of human CBP histone acetyltransferase
      Specific Activity[Varies with lot. For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.] XXX 250 pmol/min/µg assayed as production of CoA-SH from AcCoA in the presence of a peptide comprising human p53 residues 368-386. CoA-SH is determined colorimetrically by reaction with DTNB (5,5′-Dithiobis (2-nitrobenzoic acid).
      UniProt Number
      Molecular Weight~48 kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable for 12 months at -80°C from date of receipt. Avoid multiple freeze/thaw cycles.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Número de referencia GTIN
      03-189 04053252550836

      Documentation

      CBP (catalytic domain) human recombinant Certificados de análisis

      CargoNúmero de lote
      CBP (catalytic domain) human -2809583 2809583
      CBP (catalytic domain) human recombinant - 2390574 2390574
      CBP (catalytic domain) human recombinant - 3201380 3201380
      CBP (catalytic domain) human recombinant - 3537859 3537859
      CBP (catalytic domain) human recombinant - 3722793 3722793
      CBP (catalytic domain) human recombinant - 3764141 3764141
      CBP (catalytic domain) human recombinant - Q2022474 Q2022474
      CBP (catalytic domain) human recombinant -2522058 2522058
      CBP (catalytic domain) human recombinant, Recombinant Protein 2926418

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      Categorías

      Life Science Research > Proteins and Enzymes > Other Enzymes