|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||37512 Da|
|Other Names||Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PP-1A, PPP1CA, PPP1A|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding Threonine 320 of human PP1 alpha was used as an immunogen. This antibody detects PP1 alpha phosphorylated at Threonine 320.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PP1 alpha Antibody Phospho (pT320) is for research use only and 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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Provided below are standard protocols that you may find useful for product applications.
Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits (1). The coordinated and reciprocal action of serine/threonine protein kinases and phosphatases produces transient phosphorylation, a fundamental regulatory mechanism for many biological processes. PP1 is ubiquitously distributed and regulates a broad range of cellular functions, including glycogen metabolism, cell-cycle progression and muscle relaxation. PP1 has evolved effective catalytic machinery but lacks substrate specificity. Substrate specificity is conferred upon PP1 through interactions with a large number of regulatory subunits (2). It has been shown that PP1 determines the efficacy of learning and memory by limiting acquisition and favouring memory decline. When PP1 is genetically inhibited during learning, short intervals between training episodes are sufficient for optimal performance (3).
1. Cohen PT, J Cell Sci 115(Pt2):241-56, 2002.
2. Terrak M, et al. Nature 429(6993):780-4, 2004
3. Genoux D, et al. Nature 418(6901):929-30, 2002.
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