Render Target: STATIC
Render Timestamp: 2025-03-21T10:28:36.375Z
Commit: 779953b12a5930618aae6aca7c87fb286faeb1d7
XML generation date: 2025-03-07 13:14:56.250
Product last modified at: 2025-01-01T09:06:15.108Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

PME-1 (8A6-F8) Mouse mAb #29135

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 42
    Source/Isotype Mouse IgG1
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PME-1 (8A6-F8) Mouse mAb recognizes endogenous levels of total PME-1 protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant full-length mouse PME-1 protein.

    Background

    Protein phosphatase methylesterase 1 (PME-1) is an evolutionarily conserved enzyme that demethylates phosphatases (1). Post-translational modification (PTMs) of proteins is a cellular mechanism that increases the functional diversity of the proteome. Several forms of PTMs exist, including methylation and phosphorylation, the covalent addition of a methyl or phosphate group, respectively, to specific amino acids within a protein. In addition to enzymes that catalyze the addition of methyl groups or phosphates to proteins, specific enzymes that remove PTMs exist to provide an additional level of cellular regulation; methyl and phosphate PTMs are removed by methylesterases and phosphatases, respectively. Phosphoprotein phosphatase 2a (PP2A) is an essential serine/threonine phosphatase that, as part of various signal transduction pathways, regulates many fundamental cellular processes, including DNA replication, transcription, translation, metabolism, cell cycle progression, cell division, apoptosis, and development (2-4). PP2A function is regulated, in part, by phospho- and methyl modification of its catalytic subunit. PP2A is methylated at the carboxyl group of the C-terminal Leucine 309 residue by leucine carboxyl methyltransferase (LCMT). Methylation of PP2A alters its cellular localization and its ability to interact with its regulatory subunits and substrates (5-8). PP2A is demethylated by PME-1 (9,10). PME-1 KO mice are post-natal lethal, and KO tissue exhibit altered PP2A activity and phospho-proteomic profile, consistent with a critical role PME-1 plays in regulating PP2A function (11). Dysregulated PP2A activity is linked to several diseases, including certain cancers and neurodegenerative diseases like Alzheimer’s disease, suggesting that PME-1 could be the target of therapeutic intervention (12-14).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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