|Other Names||Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PP-1A, PPP1CA, PPP1A|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13424a was selected from the N-term region of PPP1CA. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. 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. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Dephosphorylates CENPA (PubMed:25556658). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5- ATG16L1 complex, thereby inhibiting autophagy (PubMed:26083323).|
|Cellular Location||Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles|
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The protein encoded by this gene is one of the threecatalytic subunits of protein phosphatase 1 (PP1). PP1 is aserine/threonine specific protein phosphatase known to be involvedin the regulation of a variety of cellular processes, such as celldivision, glycogen metabolism, muscle contractility, proteinsynthesis, and HIV-1 viral transcription. Increased PP1 activityhas been observed in the end stage of heart failure. Studies inboth human and mice suggest that PP1 is an important regulator ofcardiac function. Mouse studies also suggest that PP1 functions asa suppressor of learning and memory. Three alternatively splicedtranscript variants encoding different isoforms have been found forthis gene.
Ladha, J., et al. Cancer Res. 70(16):6437-6447(2010)Lee, J.H., et al. J. Biol. Chem. 285(32):24466-24476(2010)Nakamura, K., et al. J. Biochem. 147(4):493-500(2010)Hall, E.H., et al. J. Biol. Chem. 284(50):34713-34722(2009)Chen, S., et al. J. Biol. Chem. 284(38):25576-25584(2009)
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