Cat. # | Size | Qty. | Price |
---|---|---|---|
29135S | 100 µl |
|
REACTIVITY | H M R |
SENSITIVITY | Endogenous |
MW (kDa) | 42 |
Source/Isotype | Mouse IgG1 |
Product Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Loading of prestained molecular weight markers (#59329, 10 µl/lane) to verify electrotransfer and biotinylated protein ladder (#7727, 10 µl/lane) to determine molecular weights are recommended.
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 262
Human, Mouse, Rat
Monoclonal antibody is produced by immunizing animals with recombinant full-length mouse PME-1 protein.
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).
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