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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 Proteins (18) and Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A Kits (8) and many more products for this protein.
Showing 10 out of 88 products:
Human Monoclonal PPM1A Primary Antibody for FACS, ELISA - ABIN969556
Sun, Yu, Dotti, Shen, Tan, Savoldo, Pass, Chu, Zhang, Lu, Fu, Lin, Yang: PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation. in Cellular signalling 2008
Show all 2 references for ABIN969556
Human Monoclonal PPM1A Primary Antibody for EIA, IHC (p) - ABIN121149
Das, Helps, Cohen, Barford: Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. in The EMBO journal 1997
Show all 2 references for ABIN121149
Human Monoclonal PPM1A Primary Antibody for IP, ELISA - ABIN165454
Lin, Duan, Liang, Su, Wrighton, Long, Hu, Davis, Wang, Brunicardi, Shi, Chen, Meng, Feng: PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. in Cell 2006
Chicken Polyclonal PPM1A Primary Antibody for WB - ABIN2787379
Wu, Wang, Yang, Feng, Zhao, Yang: Expression of PTEN, PPM1A and P-Smad2 in hepatocellular carcinomas and adjacent liver tissues. in World journal of gastroenterology : WJG 2007
Mouse (Murine) Polyclonal PPM1A Primary Antibody for IP, ELISA - ABIN2000689
Soares, Marc, Reeve: Conserved eukaryotic histone-fold residues substituted into an archaeal histone increase DNA affinity but reduce complex flexibility. in Journal of bacteriology 2003
findings demonstrate a novel regulatory circuit in which STING and TBK1 (show TBK1 Antibodies) reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A dephosphorylates STING and TBK1 (show TBK1 Antibodies)
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 Antibodies) signaling in which MAN1 (show LEMD3 Antibodies) competes with transcription factors for binding to Smad2 (show SMAD2 Antibodies) and Smad3 (show SMAD3 Antibodies) and facilitates their dephosphorylation by PPM1A.
Although a non-myristoylated mutation (G2A (show GPR132 Antibodies)) of PPM1A and PPM1B (show PPM1B Antibodies) prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha (show GRK4 Antibodies).
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 Antibodies)/3 through targeting nuclear exporter RanBP3 (show RANBP3 Antibodies).
Ppm1a, through suppressing Smad2 (show SMAD2 Antibodies) 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.
The TGF-beta (show TGFB1 Antibodies)/Smad (show SMAD1 Antibodies) 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.
PPM1A is a RelA (show NFkBP65 Antibodies) phosphatase that regulates NF-kappaB (show NFKB1 Antibodies) activity and that PPM1A has tumor suppressor-like activity.
phosphatase activity toward phosphopeptide substrates by PP2Calpha and Wip1 (show PPM1D Antibodies) requires the binding of a Mg(2 (show MUC7 Antibodies))+ ion to the low-affinity site.
PPM1A negatively regulates ERK (show EPHB2 Antibodies) by directly dephosphorylating its pThr202 position early in epidermal growth factor (show EGF Antibodies) stimulation. Additional kinetic studies reveal that key residues participate in phospho-ERK (show EPHB2 Antibodies) recognition by PPM1A.
Studies indicate that phosphatase PPM1G (show PPM1G Antibodies) is a component of the spliceosome and binds to protein YB-1 (show YBX1 Antibodies) to affect alternative splicing.
PPM1A inhibits HIV-1 infection and gene expression. PPM1A depletion in resting CD4 (show CD4 Antibodies)+ T cells increases HIV-1 gene expression.
High expression of LMP2 (show PSMB9 Antibodies) and low expression of PPM1A might play an important role in the motility and invasiveness of trophoblast cells and malignant transformation of hydatidiform mole.
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