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The protein encoded by PPM1A is a member of the PP2C family of Ser/Thr protein phosphatases. Additionally we are shipping Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A Antibodies (118) and Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A Kits (10) and many more products for this protein.
Showing 10 out of 19 products:
VRK1 (show VRK1 Proteins) self-represses its activity to phosphorylate PXR (show NR1I2 Proteins) through cyclin-dependent kinase 2 (CDK2 (show CDK2 Proteins)) in high glucose conditions, resulting in the repression of the PCK1 (show PCK1 Proteins) gene. This PXR (show NR1I2 Proteins) phosphorylation was also observed in fasting mouse livers. Thus, the VRK1 (show VRK1 Proteins)-CDK2 (show CDK2 Proteins)-PXR (show NR1I2 Proteins)-PP2Calpha-SGK2 (show SGK2 Proteins) pathway can be a novel physiological cell signaling that regulates gluconeogenesis in response to glucose.
findings demonstrate a novel regulatory circuit in which STING and TBK1 (show TBK1 Proteins) reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A dephosphorylates STING and TBK1 (show TBK1 Proteins)
the studies presented here position PPM1A 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
a nuclear envelope-localized mechanism of inactivating TGF-beta (show TGFB1 Proteins) signaling in which MAN1 (show LEMD3 Proteins) competes with transcription factors for binding to Smad2 (show SMAD2 Proteins) and Smad3 (show SMAD3 Proteins) and facilitates their dephosphorylation by PPM1A.
Although a non-myristoylated mutation (G2A (show GPR132 Proteins)) of PPM1A and PPM1B (show PPM1B Proteins) prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha (show GRK4 Proteins).
we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A protein
Protein phosphatase PPM1A regulates the nuclear export of Smad2 (show SMAD2 Proteins)/3 through targeting nuclear exporter RanBP3 (show RANBP3 Proteins).
Ppm1a, through suppressing Smad2 (show SMAD2 Proteins) signaling, plays a critical role in re-epithelialization during wound healing
Molecular cloning and expression analysis of MPP alpha-2, a novel transcript detected in a differential screen of pituitary libraries (MPPalpha 2)
Protein phosphatase 1alpha is required for lung growth and morphogenesis.
Present study suggests that HBx-induced degradation of PPM1a is a novel mechanism for over-activation of TGF-beta (show TGFB1 Proteins) pathway in HCC (show FAM126A Proteins) development.
Findings show that HCV infection and replication decreased PPM1A abundance, mediated by NS3, in hepatoma cells. Compared to normal liver tissues, the expression of PPM1A was significantly decreased in the HCC tumor tissues and adjacent non-tumor tissues through its regulation by NS3 which promotes its ubiquitination and proteasomal degradation.
These data suggest that PPM1A, which had previously been shown to play a role in the antiviral response to Herpes Simplex virus infection, also governs the antibacterial response of macrophages to bacteria, or at least to Mycobacterium tuberculosis infection
establish PPM1A as a novel repressor of the SMAD3 (show SMAD3 Proteins) pathway in renal fibrosis
Report a tumor-suppressive function of PPM1A and an independent relationship to Smad4 (show SMAD4 Proteins) in pancreatic ductal adenocarcinoma.
hydrogen/deuterium exchange-mass spectrometry and molecular dynamics to characterize conformational changes in PP2Calpha between the active and inactive states
In a nested case control study of ischemic stroke, there was an epigenome-wide association for cg04985020 (PPM1A; P=1.78x10(-07)) with vascular recurrence in patients treated with aspirin.
The TGF-beta (show TGFB1 Proteins)/Smad (show SMAD1 Proteins) signaling system decreases its activity through strong negative regulation. We provide evidence for a new negative feedback loop through PPM1A upregulation.
Loss of PPM1A is associated with the development of tumor invasion in bladder cancer patients.
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 1A
, protein phosphatase 2C isoform alpha
, protein phosphatase IA
, protein phosphatase 1A (formerly 2C), magnesium-dependent, alpha isoform
, Protein phosphatase type 1A (formely 2C) Mg-dependent alpha isoform
, Protein phosphatase type 1A (formely 2C), Mg-dependent, alpha isoform
, protein phosphatase 1A, magnesium dependent, alpha isoform
, protein phosphatase 2C alpha
, protein phosphatase type 2C alpha 2
, protein phosphatase 1A, magnesium dependent, alpha