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anti-Human PPP2R2A Anticorps:
anti-Rat (Rattus) PPP2R2A Anticorps:
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Human Polyclonal PPP2R2A Primary Antibody pour WB - ABIN1881683
Li, Cai, Shouse, Piluso, Liu: A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55. dans The EMBO journal 2007
Show all 4 Pubmed References
we provide evidence that PPP2R2A represents a new miR-21 direct target and regulator of the ERK pathway and bladder cancer cell growth.
Taken together, the results suggest that miR-222 promotes tumor invasion and metastasis in thyroid cancer by targeting PPP2R2A.
PPP2R2A interacts with GFPT1/2, and leads to the phosphorylation of GFPT2, which can regulate the cellular O-GlcNAcylation in breast cancer
Data show that SAM Domain and HD Domain-Containing Protein 1 (SAMHD1) is specifically targeted by protein phosphatase 2 regulatory subunit Balpha protein (PP2A-B55alpha) holoenzymes during mitotic exit.
the data suggested that miR614 promoted cell proliferation and inhibited cell apoptosis of ovarian cancer (OC) cells by targeting PPP2R2A, and may therefore act as a potential target for OC therapy in the future.
B55alpha-PP2A mutations in acute myeloid leukemia have roles in leukemogenesis by promoting AKT T308 phosphorylation and sensitivity to AKT inhibitor-induced growth arrest
these results provide a novel insight into the role of PP2A-B55alpha as a novel meiotic and embryonic competence factor at the onset of life.
we propose that the Smad4-Pitx2-PPP2R2A axis, a new signaling pathway, suppresses the pancreatic carcinogenesis
These data unravel B55alpha as a PHD2 substrate and highlight a role for PHD2-B55alpha in the response to nutrient deprivation.
results suggest that PR55alpha promotes pancreatic cancer development by sustaining hyperactivity of multiple oncogenic signaling pathways, including AKT, ERK, and Wnt
miR-222 targets protein phosphatase 2A subunit B in bladder cancer cells.
miR-556-5p functions as an onco-miRNA and participates in prostate cancer carcinogenesis by suppressing PPP2R2A expression.
Concurrent mTORC1 inactivation and PP2A-B55alpha stimulation fuel ULK1-dependent autophagy.
Data show that breast cancer (BC) with PPP2R2A deletions are associated with worse overall survival, and the combination of altered PPP2R2A and high CCND1 expression define a subgroup of luminal-like BC patients with a high risk of relapse and death.
overexpression of miR-892a may provide a selective growth promotion for colorectal cancer cells by direct suppression of PPP2R2A expression.
miR-136 may play an important role during TGF-beta1-induced proliferation arrest by targeting PPP2R2A in keratinocytes.
Data suggest livers of biliary atresia subjects exhibit overexpression of MIR222 (microRNA 222); this appears to contribute to liver fibrosis (and in vitro cell proliferation) by targeting PPP2R2A (protein phosphatase 2A subunit B) and Akt signaling.
The suppression of B55alpha activates signaling pathways that could support leukemia cell survival.
Identification of the adenovirus E4orf4 protein binding site on the B55alpha and Cdc55 regulatory subunits of PP2A: Implications for PP2A
miR-136 promotes Erk1/2 phosphorylation through targeting PPP2R2A in NSCLC cells and suggest that it may serve as a therapeutic target in NSCLC therapy.
Data suggest IGT10 mice, diabetes type 2 model, exhibit 2 genetic defects: haploinsufficiency (heterozygosity for null allele) of insulin receptor (Insr); splice-site mutation in protein phosphatase 2 regulatory subunit B alpha (Ppp2r2a). Inheritance of either allele results in insulin resistance but not overt diabetes. Double heterozygosity leads to insulin resistance and diabetes type 2 without increase in body weight.
FBXL16 negatively regulates the activity of B55alpha-PP2A to modulate the genesis of FLK1+ progenitor cells.
Ppp2r2a is required for Connexin-43 dephosphorlyation during epidermal barrier acquisition
The B55alpha-EDD-p53 pathway is essential for cancer cell survival and tumor growth under low glutamine conditions in vitro and in vivo.
that B55alpha-dependent targeting of the PP2A holoenzyme to Akt selectively regulates Akt phosphorylation at Thr-308 to regulate cell proliferation and survival.
PP-2A is less abundant than PP-1 in the mouse eye and appear to be highly regulated by various regulatory subunits; the genes encoding PP-1alpha/beta, PP-2Aalpha/beta, PP-2A-Aalpha/beta, and PP-2A-B alpha/beta/gamma are all differentially expressed.
Phosphorylation of T231 (AT180) can negatively influence the dephosphorylation of the pS202/pT205 AT8 epitope, even without an altered PP2A pool.
The product of this gene belongs to the phosphatase 2 regulatory subunit B family. Protein phosphatase 2 is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes an alpha isoform of the regulatory subunit B55 subfamily. Alternatively spliced transcript variants have been described.
protein phosphatase 2 (formerly 2A), regulatory subunit B (PR52), alpha isoform
, serine/threonine protein phosphatase 2A, 55 KDA regulatory subunit B, alpha isoform
, serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
, PP2A subunit B isoform B55-alpha
, PP2A subunit B isoform BRA
, PP2A subunit B isoform PR55-alpha
, PP2A subunit B isoform R2-alpha
, PP2A subunit B isoform alpha
, PP2A, subunit B, B-alpha isoform
, PP2A, subunit B, B55-alpha isoform
, PP2A, subunit B, BRA isoform
, PP2A, subunit B, PR55-alpha isoform
, PP2A, subunit B, R2-alpha isoform
, protein phosphatase 2 (formerly 2A), regulatory subunit B (PR 52), alpha isoform
, protein phosphatase 2 (formerly 2A), regulatory subunit B, alpha isoform
, protein phosphatase 2A 55 kDa regulatory subunit, alpha isoform
, protein phosphatase 2, regulatory subunit B, alpha