PP1C gamma Antibody (YA1068)
(Synonyms: PP 1G; PP-1G; PP1G; PP1G_HUMAN; PP1gamma; PPP 1G; PPP1CC; PPP1CC protein; PPP1G; Protein phosphatase 1 catalytic subunit gamma isoform; Protein phosphatase 1C catalytic subunit; Protein phosphatase 1C subunit; Protein phosphatase 2C gamma isoform; Serine/threonine phosphatase 1 gamma; Serine/threonine protein phosphatase PP1 gamma catalytic subunit; Serine/threonine-protein phosphatase PP1-gamma catalytic subunit.)PP1C gamma Antibody (YA1068) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to PP1C gamma.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.3.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:500-1:1000 |
Product Details
PP1C gamma Antibody (YA1068) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to PP1C gamma.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 37 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 37 kDa
Purified recombinant human PP1C protein fragments expressed in E.coli.
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.3.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
PP1C gamma is a Protein phosphatase that associates witH2O2er 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. Dephosphorylates RPS6KB1. 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 cH2O2atin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, tH2O2gh the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Regulates the recruitment of the SKA complex to kinetochores. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Together with PPP1CA (PP1-alpha subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response. Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation. The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities. Dephosphorylates MKI67 at the onset of anaphase. The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c[1][2][3][4][5][6][7][8][9].
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Subcellular Localization
Cytoplasm; Nucleus; Nucleus, nucleolus; Nucleus, nucleoplasm; Nucleus speckle; CH2O2osome, centromere, kinetochore; Cleavage furrow; Midbody; Mitochondrion; Cytoplasm, cytoskeleton, microtubule organizing center
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Expression
Induction:Up-regulated in synovial fluid mononuclear cells and peripheral blood mononuclear cells from with rheumatoid arthritis -
Isoforms & Post-Translational Modification
P36873 has 2 isomers: P36873-1: 36984 Da (predicted); P36873-2: 38518 Da (predicted).
Phosphorylated by NEK2 -
Subunit
PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits.
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SwissProt ID
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Synonyms
PP 1G; PP-1G; PP1G; PP1G_HUMAN; PP1gamma; PPP 1G; PPP1CC; PPP1CC protein; PPP1G; Protein phosphatase 1 catalytic subunit gamma isoform; Protein phosphatase 1C catalytic subunit; Protein phosphatase 1C subunit; Protein phosphatase 2C gamma isoform; Serine/threonine phosphatase 1 gamma; Serine/threonine protein phosphatase PP1 gamma catalytic subunit; Serine/threonine-protein phosphatase PP1-gamma catalytic subunit.
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Research Field
Cell Biology
Documentation
References
[1]. Djouder N, et al. S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling. Mol Cell. 2007 Oct 12;28(1):28-40. [Content Brief]
[2]. Takagi M, et al. Ki67 antigen contributes to the timely accumulation of protein phosphatase 1γ on anaphase chromosomes. J Biol Chem. 2014 Aug 15;289(33):22877-22887. [Content Brief]
[3]. Lee JH, et al. Identification and characterization of a novel human PP1 phosphatase complex. J Biol Chem. 2010 Aug 6;285(32):24466-76. [Content Brief]
[4]. Schmutz I, et al. Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock. PLoS One. 2011;6(6):e21325. [Content Brief]
[5]. Sivakumar S, et al. Phosphatase-regulated recruitment of the spindle- and kinetochore-associated (Ska) complex to kinetochores. Biol Open. 2017 Nov 15;6(11):1672-1679. [Content Brief]
[6]. Nie H, et al. Phosphorylation of FOXP3 controls regulatory T cell function and is inhibited by TNF-α in rheumatoid arthritis. Nat Med. 2013 Mar;19(3):322-8. [Content Brief]
[7]. Wies E, et al. Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling. Immunity. 2013 Mar 21;38(3):437-49. [Content Brief]
[8]. Liau NPD, et al. Structural basis for SHOC2 modulation of RAS signalling. Nature. 2022 Sep;609(7926):400-407. [Content Brief]
[9]. Kwon JJ, et al. Structure-function analysis of the SHOC2-MRAS-PP1C holophosphatase complex. Nature. 2022 Sep;609(7926):408-415. [Content Brief]