|Other Names||Protein phosphatase 1 regulatory subunit 3D, Protein phosphatase 1 regulatory subunit 6, PP1 subunit R6, Protein phosphatase 1-binding subunit R6, PPP1R3D, PPP1R6|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP13440a was selected from the N-term region of PPR3D. 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||Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis.|
|Tissue Location||Expressed in all tissues tested. High expression in skeletal muscle and heart|
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Provided below are standard protocols that you may find useful for product applications.
Phosphorylation of serine and threonine residues inproteins is a crucial step in the regulation of many cellularfunctions ranging from hormonal regulation to cell division andeven short-term memory. The level of phosphorylation is controlledby the opposing actions of protein kinases and proteinphosphatases. Protein phosphatase 1 (PP1) is 1 of 4 majorserine/threonine-specific protein phosphatases which have beenidentified in eukaryotic cells. PP1 associates with variousregulatory subunits that dictate its subcellular localization andmodulate its substrate specificity. Several subunits that targetPP1 to glycogen have been identified. This gene encodes aglycogen-targeting subunit of PP1.
Wu, C., et al. Proteomics 7(11):1775-1785(2007)Deloukas, P., et al. Nature 414(6866):865-871(2001)Armstrong, C.G., et al. FEBS Lett. 418 (1-2), 210-214 (1997) :Allen, P.B., et al. Proc. Natl. Acad. Sci. U.S.A. 94(18):9956-9961(1997)
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