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Human Monoclonal PPP1CA Primary Antibody pour WB - ABIN534429
Gao, Zhou, Xie, Zhang, Rahmeh, Huang, Lee, Lee: Protein phosphatase-1 is targeted to DNA polymerase delta via an interaction with the p68 subunit. dans Biochemistry 2008
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Human Monoclonal PPP1CA Primary Antibody pour ELISA, WB - ABIN532972
Cohen: Protein phosphatase 1--targeted in many directions. dans Journal of cell science 2002
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Human Monoclonal PPP1CA Primary Antibody pour ELISA, WB - ABIN969360
Chen, Kesler, Paschal, Balk: Androgen receptor phosphorylation and activity are regulated by an association with protein phosphatase 1. dans The Journal of biological chemistry 2009
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Human Monoclonal PPP1CA Primary Antibody pour ELISA, WB - ABIN969359
Luo, Peterson, Garcia, Coombs, Kofahl, Heinrich, Shabanowitz, Hunt, Yost, Virshup: Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex. dans The EMBO journal 2007
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Mouse (Murine) Polyclonal PPP1CA Primary Antibody pour IHC, WB - ABIN3023151
Wu, Zhang, Peirats-Llobet, Belda-Palazon, Wang, Cui, Yu, Rodriguez, An: Ubiquitin Ligases RGLG1 and RGLG5 Regulate Abscisic Acid Signaling by Controlling the Turnover of Phosphatase PP2CA. dans The Plant cell 2016
Data show the preparation, characterization, and structure of iron-bound protein phosphatase-1 alpha (PP1alpha) in inactive and active states.
In contrast, substrate trapping was barely detected with active PP1-RIPPO fusions or with nonfused PP1 or RIPPO subunits. Our results suggest that hypoactive fusions of PP1 subunits represent an easy-to-use tool for substrate identification of individual holoenzymes.
Study reports a S6K/PP1alpha/B-Raf pathway that activates MAPK signaling in PI3K/AKT-driven cancers and is opposed by the promyelocytic leukemia (PML) tumor suppressor. Its importance in regulating prostate cancer cell migration and invasion and in metastatic human prostate cancer is demonstrated.
Downregulation of the expression of DUSP1 or protein phosphatase 1 led to a decline in the beta2adrenergic receptormediated dephosphorylation of ERK1/2
human plasma protects against endothelial cell apoptosis through sustained BAD phosphorylation, which is achieved by, at least in part, a novel interaction between PP1 with PAI1.
Data show that protein phosphatase-1 alpha (PP1alpha) is required to maintain checkpoint kinase 1 (CHK1) in a dephosphorylated state and for the accelerated replication fork progression in Spi1/PU.1 transcription factor-overexpressing cells.
Data suggest that protein phosphatase 1, catalytic subunit, alpha isoform (PPP1CA) is a candidate sero-diagnostic and prognostic marker for badder cancer (BC).
Rif1 can mediate MCM dephosphorylation at replication forks and that the stability of dephosphorylated replisomes strongly depends on Chk1 activity.
Data, including data from studies using cells from knockout mice, suggest that gasotransmitter H(2)S up-regulates eIF2a phosphorylation by inhibiting PPP1CA via persulfidation, which in turn leads to transient suppression of global translation and activation of Atf4 expression. (eIF2a = eukaryotic initiation factor-2alpha; PPP1CA = protein phosphatase 1 catalytic subunit alpha; Atf4 = activating transcription factor 4)
Protein phosphatase 1 (PP1) forms stable complexes with PP1-interacting proteins (PIPs) that guide the phosphatase throughout its life cycle and control its fate and function.
The authors found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism.
this study shows a pivotal role for PP1 in impeding IRF7-mediated IFN-alpha production in host immune responses
The data support a model where Cdc7 (de)phosphorylation is the molecular switch for the activation and inactivation of DNA replication in mitosis, directly connecting Cdc7 and PP1a/Cdk1 to the regulation of once-per-cell cycle DNA replication in mammalian cells.
These results indicate that PP1 is recruited to the extracellular calcium-dependent E-cadherin-catenin-PIP5K1a complex in the plasma membrane to activate PIP5K1a, which is required for PLC-g1 activation leading to keratinocyte differentiation.
Data suggest that targeting protein phosphatase 1 catalytic subunit (PP1alpha) or the androgen receptor AR-PP1alpha interaction may be effective in castration-resistant prostate cancer (CRPC).
Both PP-1 and PP-2A are directly involved in regulating eye development, and are aberrantly expressed in cataract and glaucoma patients. (Review)
Data suggest that activation of TAZ (tafazzin) inhibits adipogenesis in mesenchymal stem cells; interaction of TAZ and protein phosphatases (PP1A, PP2A) up-regulates dephosphorylation and transport of TAZ to cell nucleus.
ATG16L1 as a bona fide physiological CSNK2 and PPP1 substrate, which reveals a novel molecular link from CSNK2 to activation of the autophagy-specific ATG12-ATG5-ATG16L1 complex and autophagy induction
PARD3 promotes interaction between PP1A and LATS1 to induce LATS1 dephosphorylation and inactivation,leading to dephosphorylation and activation of TAZ
activation of the Nherf1-PP1alpha-TAZ pathway in osteoblasts is targeted by histone deacetylase inhibitors
These findings describe an original mechanism involving a phosphatase in the regulation of aldosterone signaling and provide new and important insights into the molecular mechanism underlying the MR turnover.
Data, including data from studies using transgenic/knockout mice, suggest that Ppp1ca and Gnb1 interact in quiescent platelets; then, Ppp1ca and Plcb3 interact during platelet aggregation; thus, Gnb1 enlists Ppp1ca to modulate G protein-coupled receptor signaling. (Ppp1ca = protein phosphatase 1, catalytic subunit alpha; Gnb1 = guanine nucleotide-binding protein, subunit beta-1; Plcb3 = phospholipase C, subunit beta-3)
Ang IV functions via regulating the activity of PP1
Cell surface expression of the major amyloid-beta peptide (Abeta)-degrading enzyme, neprilysin, depends on phosphorylation by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a.
analysis of selective regulation of NR2B by protein phosphatase-1 for the control of the NMDA receptor in neuroprotection
alteration of lipid rafts is an early event in the apoptotic cascade indirectly induced by interleukin-4 deprivation via PP1alpha activation, dephosphorylation of cytoplasmic Bad, and caspase activation
Data show that Nck (isoforms 1 and 2) as a component of the CReP/PP1c holophosphatase complex contributes to maintain eIF2alpha in a hypophosphorylated state, and modulates translation and eIF2alpha signaling in response to ER stress.
Our system may be useful for the elucidation of the mechanism of morphological maturation of neuronal cells such as dorsal root ganglion neurons that express SREC-I during early development.
Ppp1ca was identified in the study.
overexpression of two out of five PPP1CA alternative spliced variants reduced tumor cell growth and the downregulation of the protein to hemizygosity increased the anchorage-independent growth
Results demonstrate myofilament regulation by protein phosphatase type 1 alpha and CapZ, and support the concept that cardiac Z-discs are vital components in intracellular signalling.
PP-1 is more abundant than PP-2A in the mouse eye; the genes encoding PP-1alpha/beta, PP-2Aalpha/beta, PP-2A-Aalpha/beta, and PP-2A-Balpha/beta/gamma are all differentially expressed.
Par-3 functions as a scaffold, coordinating both serine/threonine kinases and the PP1alpha phosphatase
Our findings clearly confirm that contextual memory formation involves CREB and PP1 as positive and negative regulators, respectively, and show for the first time that temporal memory formation shares this mechanism.
The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.
protein phosphatase 1, catalytic subunit, alpha isoform
, serine/threonine protein phosphatase PP1-alpha 1 catalytic subunit
, serine/threonine-protein phosphatase PP1-alpha catalytic subunit
, Protein phosphatase type 1 alpha, catalytic subunit
, protein phosphatase-1d
, protein phosphatase 1, catalytic subunit, alpha
, PP1 alpha
, protein phosphatase 1 alpha