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Human Polyclonal PPP1CC Primary Antibody for ICC, IF - ABIN442812
Werle, Chen, Xu, Zhao, He, Lu, Cui, Liang, Li, Xu: Liver kinase B1 regulates the centrosome via PLK1. in Cell death & disease 2014
PP1 promotes dephosphorylation of nNOS serine-852 leading to nitroc oxide and hydrogen peroxide production and endothelium-dependent vasodilation.
These findings provide novel evidence for a role of miRNAs in memory formation and suggest the implication of PP1 in miRNAs processing in the adult brain.
NEK1 phosphorylates PP1gamma, leading to the dephosphorylation of WAPL, which, in turn, results in its retention on chromosome cores to promote loss of cohesion at the end of prophase I in mammals.
The interaction between PPP1CC2 and AKAP4 in human spermatozoa.
DNA modification methylase inhibitor 5-aza-2'-deoxycytidine restrains the expression of PP1gamma which is related to learning and memory in mice.
Aurkb phosphorylates Oct4(S229) during G2/M phase, leading to the dissociation of Oct4 from chromatin, whereas PP1 binds Oct4 and dephosphorylates Oct4(S229) during M/G1 transition, which resets Oct4-driven transcription for pluripotency and the cell cycle.
avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.
PP1 directly interacts with IRF3 and dephosphorylates IRF3 at Ser385 and Ser396, resulting in the suppression of TLR- and RLR-triggered IFN-beta production.
The endogenous Ppp1cc promoter normally functions in the testis to maintain a sufficient level of PPP1CC2 expression for normal spermatogenesis to occur.
In mouse testis, PPP1CC2 can form a complex with TSSK1 mediated by the direct interaction of each with the kinase substrate protein TSKS. Interaction between PPP1CC2 and TSKS is mediated through an RVxF docking motif on the TSKS surface.
Spermatogenic defects observed in the global Ppp1cc knockout mice and in mice expressing low levels of PPP1CC2 in testis are due to compromised functions of PPP1CC2 in meiotic and postmeiotic germ cells.
PP1cgamma mutant sperm are unable to support development to the blastocyst stage, resulting in arrested development either before or just after compaction.
The present study focused on TGF-beta-modulation of paxillin and the serine/threonine protein phosphatase PP-1, and the impact on cellular motility.
Results identify protein phosphatase 1 (PP1) as regulator of period and light-induced resetting of the mammalian circadian clock.
Present results demonisterated that not only phosphorylation but also dephosphorylation is a major mechanism involved in learning and memory. Therefore, inhibition of hippocampal phosphatase activity might improve learning and memory.
Thrombin-stimulated PP1cgamma(-/-) platelets showed decreased alpha(IIb)beta(3) activation despite comparable levels of alpha(IIb)beta(3), PAR3, PAR4 expression and normal granule secretion.
glutamate receptors type 1a, 5a, and 5b bind to protein phosphatase 1C
there is a protein phosphatase-1gamma1 isoform selectivity determinant in dendritic spine-associated neurabin
the interaction between Spz1 and PP1cgamma2 may be required for proper regulation of spermatogenesis and fertility in males
PP1gamma2 is involved in sperm tail morphogenesis.
Here the authors show how Ki-67 and RepoMan form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase during mitosis.
Data suggest that PPP1CC catalyzes hydrolysis of an assortment of substrates (aryl methylphosphonates, fluorophosphate esters, phosphorothioate esters, phosphodiesters); conservative mutation of R221 to K results in a mutant that is more effective catalyst toward monoanionic substrates; PPP1CC does not catalyze the hydrolysis of a sulfate ester, which is unexpected.
PP1gamma is upregulated in hepatocellular carcinoma (HCC) cell lines and HCC specimens and promotes cancer cell proliferation through regulation of p53. High expression of PP1gamma in HCC cells contributed to doxorubicin resistance.
knock-down of PP1gamma alleviates glioma proliferation by reducing p65 transportation into the nucleus.
PP1gamma may be a novel target of the HPV-16 oncoproteins and indicate that it might be a potential novel biomarker for HPV-16 induced malignancy.
Although no obvious defects in the progression of mitosis were observed, the timing of dephosphorylation of the mutant Ki67 in anaphase was delayed, indicating that Ki67 itself is one of the substrates of PP1gamma-Ki67.
the lipin-1 N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma
Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor.
PP-1alpha and PP-1gamma not only antagonize each other in lung cancer cells, but also display differential functions in tumorigenicity.
PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells.
Findings indicate that phosphatases PP1alpha and PP1gamma are key regulators of RIG-I and MDA5 antiviral signaling.
When the Px(T)PxR motif is deleted or mutated via insertion of a phosphorylation site mimic (T311D), PP-1c fails to bind to all three ASPP proteins, ASPP1, ASPP2 and iASPP.
Depletion of PP1gamma enhances the localization of the SMN complex and snRNPs to Cajal bodies.
NUAK1 and PPP1CC are identified as positional candidate loci for skeletal muscle strength phenotypes.
The counteracting Nek2A and PP1gamma activities on the centrosome linker are controlled by Plk1.
The ataxia telangiectasia, mutated and Rad3-related-Chk1 axis regulates H3-pThr 11 dephosphorylation on DNA damage, at least in part by the activation of PP1gamma through Chk1-dependent inhibition of cyclin dependent kinases.
mammalian Wdr82 functions in a variety of cellular processes; PTW/PP1 phosphatase complex (PNUTS, Tox4, Wdr82, PP1) has a role in the regulation of chromatin structure during the transition from mitosis into interphase
gamma isoform of the human protein phosphatase-1 catalytic subunit (PP1c gamma) as a high affinity in vitro target of phosphatidic acid
Nek2.PP1C complex is regulated by Inh2 via inhibition of phosphatase activity to initiate centrosome separation
Tat might function as a nuclear regulator of PP1 and interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat
The protein encoded by this gene belongs to the protein phosphatase family, PP1 subfamily. PP1 is an ubiquitous serine/threonine phosphatase that regulates many cellular processes, including cell division. It is expressed in mammalian cells as three closely related isoforms, alpha, beta/delta and gamma, which have distinct localization patterns. This gene encodes the gamma isozyme. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
protein phosphatase 1, catalytic subunit, gamma isoform
, serine/threonine-protein phosphatase PP1-gamma catalytic subunit
, PP1C gamma 1
, PP1C gamma 2
, protein phosphatase 1C catalytic subunit
, serine/threonine phosphatase 1 gamma
, protein serine-threonine phosphatase catalytic subunit PP-1b
, protein phosphatase type 1 catalytic subunit gamma isoform
, protein phosphatase 1 gamma 1
, protein phosphatase 1-gamma 1
, serine/threonine-protein phosphatase PP1-gamma catalytic subunit A