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anti-Human PPP2R4 Antibodies:
anti-Mouse (Murine) PPP2R4 Antibodies:
anti-Rat (Rattus) PPP2R4 Antibodies:
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Human Polyclonal PPP2R4 Primary Antibody for IHC, WB - ABIN6674249
Jiang, Cao, Wang, Li, Liu, Lv, Li, Mi: Cysteine transporter SLC3A1 promotes breast cancer tumorigenesis. in Theranostics 2017
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Human Polyclonal PPP2R4 Primary Antibody for IHC, WB - ABIN5663970
Wang, Gan, Wang, Wu, Cao, Zhu, Xu, Wang, Han, Li, Ye, Zhao, Mi: Cancer-associated Fibroblasts Promote Irradiated Cancer Cell Recovery Through Autophagy. in EBioMedicine 2017
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Human Monoclonal PPP2R4 Primary Antibody for ICC, FACS - ABIN969557
Yoon, Jun, Park, Jun Yoo, Moon, Soon Baik, Kim, Kim, Kim, Koh, Taek Lee, You: Optimal suppression of protein phosphatase 2A activity is critical for maintenance of human embryonic stem cell self-renewal. in Stem cells (Dayton, Ohio) 2010
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Human Polyclonal PPP2R4 Primary Antibody for ChIP, WB - ABIN2668597
Fellner, Lackner, Hombauer, Piribauer, Mudrak, Zaragoza, Juno, Ogris: A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo. in Genes & development 2003
Cow (Bovine) Polyclonal PPP2R4 Primary Antibody for ELISA, WB - ABIN542458
Gushiken, Patel, Liu, Pradhan, Bergeron, Peng, Vijayan: Protein phosphatase 2A negatively regulates integrin alpha(IIb)beta(3) signaling. in The Journal of biological chemistry 2008
PP2A is critical in driving pulmonary arterial hypertension (PAH), and berberine (BBR) may alleviate PAH via PP2A signaling pathways, thereby offering a potential therapeutic option for PAH
Low PP2A expression is associated with chronic obstructive pulmonary disease
This review discusses the latest findings about PP2A dysregulation in Alzheimer and Parkinson diseases and possible interplay between this phosphatase and insulin signaling pathways. [review]
PP2A was highly expressed in human periprosthetic interface membranes with aseptic loosening and murine osteolysis model. PP2A inhibition effectively alleviated titanium particle-induced bone destruction and decreased osteoclast numbers.
Here we show that C. trachomatis prevents activation of the key DNA damage response mediator ATM by preventing the release from PP2A, leading to a complete absence of homologous recombination repair in host cells.
study reveals that KIAA1199 promotes metastasis of colorectal cancer cells via microtubule destabilization regulated by a PP2A/stathmin pathway, and suggests that KIAA1199 may be a promising target for preventing metastasis in colorectal cancer.
PP2A methylation is associated with cancer.
the current study demonstrated that PP2A activation promoted the migration of astrocytes and the underlying mechanism may be associated with the p38 signaling pathway.
High PP2A expression is associated with chordoma.
PP2A dephosphorylates MYPT1(pThr696) and thereby stimulates MP activity inducing dephosphorylation of eNOS(pThr497) and the 20 kDa myosin II light chains.
Study reveals the mechanism controlling abscission through integration of Aurora B kinase and B56-bound PP2A phosphatase activities on the kinesin motor protein MKlp2. MKlp2 is an essential protein for promoting abscission, which may regulate tethering and stabilizing of the PM to the microtubule cytoskeleton at the intercellular bridge through its previously uncharacterized lipid association motif.
These results suggest that loss of specific PP2A regulatory subunits is functionally important in breast tumourigenesis, and support strategies to enhance PP2A activity as a therapeutic approach in breast cancer.
High expression of PP2A is associated with cisplatin resistant gastric cancer.
Study identifies Eya3 as a regulator of PP2A, a major cellular Ser/Thr phosphatase, and uncovers a mechanism of controlling the stability of a critical oncogene, c-Myc.
Authors demonstrated CFTR and PP2AA interact in the cytosol, resulting in PP2A complex inactivation and increased degradation of PP2A substrates via the lysosomal/proteasome pathway.
Together, the results suggest a complex antagonistic interplay between the control of ARPP-16 by MAST3 and PKA that creates a mechanism whereby cAMP mediates PP2A disinhibition.
An imbalanced regulation in protein kinases and protein phosphatases is the direct cause of tau hyperphosphorylation in Alzheimer's disease; GSK-3beta and PP2A are the most implicated. (Review)
Isoliensinine suppresses NF-kappaB in hepatocellular carcinoma cells through impairing PP2A/I2PP2A interaction and stimulating PP2A-dependent p65 dephosphorylation at Ser536
BIR domain of XIAP activated the protein phosphatase 2 (PP2A) activity by decreasing the phosphorylation of PP2A at Tyr307 in its catalytic subunit, PP2A-C. Such activated PP2A prevented the deviant phosphorylation and activation of MAPK kinases/MAPKs, their downstream effector c-Jun; and in turn inhibiting transcription of c-Jun-regulated miR-200a
T-type channel signaling is redirected towards the activation of the kinase Akt1, leading to increased expression of the anti-apoptotic protein survivin, and a decrease in the pro-apoptotic mediator FoxO3A. Finally, in iPAH cells, Akt1 is no longer able to regulate caspase 9 activation, whereas T-type channel overexpression reverses PP2A defect in iPAH cells but reinforces the deleterious effects of Akt1 activation
Evidence for PPP2R4 as a haploinsufficient tumor suppressor gene, defining a high-penetrance genetic mechanism for PP2A inhibition in human cancer.
data indicate that PTPalpha and FAK, which are enriched in FAs, interact with IP3R1 at adjacent ER sites to spatially sequester IL-1-induced Ca(2+) signalling
findings show that ectopic expression of the phosphotyrosyl phosphatase activator PTPA induces cell death in mammalian cells via a mechanism involving caspase-3-dependent apoptosis
oxidative stress regulates the phosphorylation status of nonribosomal rpS3 by both activating PKCdelta and blocking the PP2A interaction with rpS3
results suggested that PPFIA1 functioned with PP2A to promote the dephosphorylation of Kif7, triggering Kif7 localization to the tips of primary cilia and promoting Gli transcriptional activity.
Protein phosphatase 2A is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2A holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B' family. This gene encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A. Alternative splicing results in multiple transcript variants encoding different isoforms.
PP2A phosphatase activator
, PP2A subunit B' isoform PR53
, phosphotyrosyl phosphatase activator
, protein phosphatase 2A, regulatory subunit B' (PR 53)
, serine/threonine-protein phosphatase 2A activator
, serine/threonine-protein phosphatase 2A regulatory subunit B'
, PP2A, subunit B', PR53 isoform
, serine/threonine-protein phosphatase 2A regulatory subunit 4
, protein tyrosine phosphatase, receptor type, A
, protein phosphatase 2 regulatory subunit 4
, protein phosphatase 2A activator, regulatory subunit 4
, protein phosphatase 2A regulatory subunit 4
, protein phosphatase 2A, regulatory subunit B (PR 53)
, protein phosphatase 2 phosphatase activator L homeolog
, protein phosphatase 2A regulatory subunit 4 L homeolog