|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||37187 Da|
|Other Names||Serine/threonine-protein phosphatase PP1-beta catalytic subunit, PP-1B, PPP1CD, PPP1CB|
|Target/Specificity||A synthetic peptide corresponding to residues on human PP1 beta was used as an immunogen.|
|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 beta Antibody 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 (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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. 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).|
|Cellular Location||Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. 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 (Ser/Thr) 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 favoring 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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