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Data, including data from studies using transgenic/knockout mice, suggest that Ppp1ca and Gnb1 (show GNB1 ELISA Kits) interact in quiescent platelets; then, Ppp1ca and Plcb3 (show PLCB3 ELISA Kits) interact during platelet aggregation; thus, Gnb1 (show GNB1 ELISA Kits) enlists Ppp1ca to modulate G protein-coupled receptor (show GPR34 ELISA Kits) signaling. (Ppp1ca = protein phosphatase 1 (show PPP1CB ELISA Kits), catalytic subunit alpha; Gnb1 (show GNB1 ELISA Kits) = guanine nucleotide-binding protein (show TRIM23 ELISA Kits), subunit beta-1; Plcb3 (show PLCB3 ELISA Kits) = phospholipase C (show PLC ELISA Kits), subunit beta-3)
findings demonstrate a novel regulatory circuit in which STING and TBK1 (show TBK1 ELISA Kits) reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A (show PPM1A ELISA Kits) dephosphorylates STING and TBK1 (show TBK1 ELISA Kits)
the studies presented here position PPM1A (show PPM1A ELISA Kits) as a new player in the wound healing-inflammation-angiogenesis axis in mouse, reveal its crucial role in homeostasis on injury, and highlight its potential as a therapeutic mediator in pathologic conditions
Ang (show ANG PLURAL_@12788@) IV functions via regulating the activity of PP1 (show PPP1CC PLURAL_@12788@)
a nuclear envelope-localized mechanism of inactivating TGF-beta (show TGFB1 ELISA Kits) signaling in which MAN1 (show LEMD3 ELISA Kits) competes with transcription factors for binding to Smad2 (show SMAD2 ELISA Kits) and Smad3 (show SMAD3 ELISA Kits) and facilitates their dephosphorylation by PPM1A (show PPM1A ELISA Kits).
Although a non-myristoylated mutation (G2A) of PPM1A (show PPM1A ELISA Kits) and PPM1B (show PPM1B ELISA Kits) prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha (show GRK4 ELISA Kits).
we found that PPM1A (show PPM1A ELISA Kits) mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A (show PPM1A ELISA Kits) protein
Cell surface expression of the major amyloid-beta peptide (Abeta (show APP ELISA Kits))-degrading enzyme, neprilysin (show MME ELISA Kits), depends on phosphorylation by mitogen-activated protein kinase (show MAPK1 ELISA Kits)/extracellular signal-regulated kinase kinase (MEK (show MDK ELISA Kits)) and dephosphorylation by protein phosphatase 1a (show PPM1A ELISA Kits).
analysis of selective regulation of NR2B (show GRIN2B ELISA Kits) by protein phosphatase-1 (show PPP1CB ELISA Kits) for the control of the NMDA receptor in neuroprotection
Protein phosphatase PPM1A (show PPM1A ELISA Kits) regulates the nuclear export of Smad2 (show SMAD2 ELISA Kits)/3 through targeting nuclear exporter RanBP3 (show RANBP3 ELISA Kits).
establish PPM1A (show PPM1A ELISA Kits) as a novel repressor of the SMAD3 (show SMAD3 ELISA Kits) pathway in renal fibrosis
Data, including data from studies using cells from knockout mice, suggest that gasotransmitter H(2)S up-regulates eIF2a (show EIF2S1 ELISA Kits) phosphorylation by inhibiting PPP1CA via persulfidation, which in turn leads to transient suppression of global translation and activation of Atf4 (show ATF4 ELISA Kits) expression. (eIF2a (show EIF2S1 ELISA Kits) = eukaryotic initiation factor-2alpha (show EIF2S1 ELISA Kits); PPP1CA = protein phosphatase 1 catalytic subunit alpha; Atf4 (show ATF4 ELISA Kits) = activating transcription factor 4 (show ATF4 ELISA Kits))
Report a tumor-suppressive function of PPM1A (show PPM1A ELISA Kits) and an independent relationship to Smad4 (show SMAD4 ELISA Kits) in pancreatic ductal adenocarcinoma.
Protein phosphatase 1 (show PPP1CB ELISA Kits) (PP1 (show PPA1 ELISA Kits)) forms stable complexes with PP1 (show PPA1 ELISA Kits)-interacting proteins (PIPs (show GPRASP1 ELISA Kits)) that guide the phosphatase throughout its life cycle and control its fate and function.
The authors found that RNA recognition motif 1 (RRM1 (show RRM1 PLURAL_@12788@)) in SRSF1 (show SRSF1 PLURAL_@12788@) binds PP1 (show PPA1 PLURAL_@12788@) and represses its catalytic function through an allosteric mechanism.
this study shows a pivotal role for PP1 (show PPA1 ELISA Kits) in impeding IRF7 (show IRF7 ELISA Kits)-mediated IFN-alpha (show IFNA ELISA Kits) production in host immune responses
hydrogen/deuterium exchange-mass spectrometry and molecular dynamics to characterize conformational changes in PP2Calpha (show PPM1A ELISA Kits) between the active and inactive states
In a nested case control study of ischemic stroke, there was an epigenome-wide association for cg04985020 (PPM1A (show PPM1A ELISA Kits); P=1.78x10(-07)) with vascular recurrence in patients treated with aspirin.
The data support a model where Cdc7 (show CDC7 ELISA Kits) (de)phosphorylation is the molecular switch for the activation and inactivation of DNA replication in mitosis, directly connecting Cdc7 (show CDC7 ELISA Kits) and PP1a/Cdk1 (show CDK1 ELISA Kits) to the regulation of once-per-cell cycle DNA replication in mammalian cells.
These results indicate that PP1 (show PPA1 ELISA Kits) is recruited to the extracellular calcium-dependent E-cadherin (show CDH1 ELISA Kits)-catenin-PIP5K1a complex in the plasma membrane to activate PIP5K1a, which is required for PLC (show HSPG2 ELISA Kits)-g1 activation leading to keratinocyte differentiation.
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding distinct isoforms have been described.
Protein phosphatase type 1 alpha, catalytic subunit
, protein phosphatase 1, catalytic subunit, alpha isoform
, serine/threonine-protein phosphatase PP1-alpha catalytic subunit
, protein phosphatase 1, catalytic subunit, alpha
, serine/threonine protein phosphatase PP1-alpha 1 catalytic subunit
, protein phosphatase-1d
, protein phosphatase 1, catalytic subunit, beta isoform
, protein phosphatase-1a
, serine/threonine-protein phosphatase PP1-beta catalytic subunit
, Mpp alpha
, protein phosphatase 1A
, protein phosphatase 2C isoform alpha
, protein phosphatase IA
, protein phosphatase 1A (formerly 2C), magnesium-dependent, alpha isoform
, protein phosphatase 2C alpha