17-301 | PP1/PP2A Toolbox

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      Replacement Information

      Key Specifications Table

      Key Applications
      Catalogue Number17-301
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionPP1/PP2A Toolbox
      Overviewfor the selective in vitro dephosphorylation of proteins
      Product Information
      • PP1, Catalog #14-110B
      • PP2A, Catalog #14-111B
      • PHI-1, Catalog #19-161
      • Okadaic Acid, Catalog #19-130B
      • Calyculin A, Catalog #19-139
      • Protein Phos. Dilution Buffer, #20-169
      ApplicationPP1/PP2A Toolbox for the selective in vitro dephosphorylation of proteins.
      Key Applications
      • Phosphatase Assay
      Biological Information
      Entrez Gene Number
      Entrez Gene SummaryThe protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.
      Gene Symbol
      • PPP1CA
      • PP-1A
      • MGC15877
      • MGC1674
      • PPP1A
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P62136 # Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II.
      COFACTOR: Binds 1 iron ion per subunit (By similarity). & Binds 1 manganese ion per subunit (By similarity).
      SIZE: 330 amino acids; 37512 Da
      SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A and PPP1R12B mediate binding to myosin. PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen. Interacts with PPP1R9A and PPP1R9B (By similarity). Interacts with PPP1R7.
      SUBCELLULAR LOCATION: Cytoplasm (By similarity).
      SIMILARITY: SwissProt: P62136 ## Belongs to the PPP phosphatase family. PP-1 subfamily.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceRoutinely evaluated by using PP1 and/or PP2A in each dephosphorylation reaction.
      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
      Packaging Information
      Material Size1 kit
      Transport Information
      Supplemental Information


      Certificates of Analysis

      TitleLot Number
      PP1/PP2A Toolbox - 2376444 2376444
      PP1/PP2A Toolbox - 1953338 1953338
      PP1/PP2A Toolbox - 20319 20319
      PP1/PP2A Toolbox - 23656 23656
      PP1/PP2A Toolbox - 24175 24175
      PP1/PP2A Toolbox - 27263 27263
      PP1/PP2A Toolbox - DAM1460108 DAM1460108
      PP1/PP2A Toolbox - DAM1524118 DAM1524118
      PP1/PP2A Toolbox - DAM1739319 DAM1739319
      PP1/PP2A Toolbox - JBC1393229 JBC1393229


      Reference overviewPub Med ID
      Phosphorylation status of nuclear ribosomal protein S3 is reciprocally regulated by protein kinase C{delta} and protein phosphatase 2A.
      Tae-Sung Kim,Hag Dong Kim,Hyun-Seock Shin,Joon Kim
      The Journal of biological chemistry  284  2009

      Show Abstract Full Text Article
      19458393 19458393
      Transcriptional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB.
      Hagiwara, M, et al.
      Cell, 70: 105-13 (1992)  1992

      Show Abstract
      1352481 1352481
      Protein phosphatases: recent progress.
      Shenolikar, S and Nairn, A C
      Adv. Second Messenger Phosphoprotein Res., 23: 1-121 (1991)  1991

      1847640 1847640
      Protein kinase activity closely associated with a reconstituted calcium-activated potassium channel.
      Chung, S K, et al.
      Science, 253: 560-2 (1991)  1991

      1857986 1857986
      Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors.
      DeFranco, D B, et al.
      Mol. Endocrinol., 5: 1215-28 (1991)  1991

      Show Abstract
      1663212 1663212
      Sequence homologies between type 1 and type 2A protein phosphatases.
      Johnson, G L, et al.
      Mol. Endocrinol., 1: 745-8 (1987)  1987

      Show Abstract
      2856400 2856400
      Phosphorylase phosphatase catalytic subunit. Evidence that the Mr = 33,000 enzyme fragment is derived from a native protein of Mr = 70,000.
      Brautigan, D L, et al.
      J. Biol. Chem., 260: 4295-302 (1985)  1985

      Show Abstract
      2984200 2984200
      Separation of rabbit liver latent and spontaneously active phosphorylase phosphatases by chromatography on heparin-sepharose.
      Erdödi, F, et al.
      Biochem. Biophys. Res. Commun., 128: 705-12 (1985)  1985

      Show Abstract
      2986623 2986623
      The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities.
      Ingebritsen, T S and Cohen, P
      Eur. J. Biochem., 132: 255-61 (1983)  1983

      Show Abstract
      6301824 6301824