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Human PPP2R1A Protein expressed in Wheat germ - ABIN1316014
Lao, Yusoff, Chandramouli, Philp, Fong, Jackson, Saw, Yu, Guy: Direct binding of PP2A to Sprouty2 and phosphorylation changes are a prerequisite for ERK inhibition downstream of fibroblast growth factor receptor stimulation. in The Journal of biological chemistry 2007
In addition, 6 other cancer-associated genes (BRAF, NRAS, HRAS, ERK1, ERK2 and PTEN) were also analyzed. In total, four somatic mutations were identified in three out of 101 ovarian endometriotic lesions (4%, 4/101), including a KRAS p.G12V, a PPP2R1A p.S256F and two ARID1A nonsense mutations (p.Q403* and p.G1926*); while no mutations were identified in the remaining 7 genes (BRAF, NRAS, HRAS, ERK1, ERK2, PTEN and PIK3CA)
PP2A controls mitotic exit through EG5 dephosphorylation.
RAB9 competes with the catalytic subunit PPP2CA in binding to PPP2R1A. This competitive association has an important role in controlling the PP2A catalytic activity.
Total PP2A activity and PPP2R1A-associated PP2Ac activity were significantly increased in cells overexpressing PPP2R1A-WT. In addition, overexpression of PPP2R1A-WT increased cell proliferation in vitro and tumor growth in vivo
PPP2R1A mutations occur in a subset of gastrointestinal stromal tumors and are associated with a high malignant potential that leads to decreased disease-free survival and overall survival
Results demonstrated that the promotive effect of eEF-2K on glycolysis resulted from the kinase-mediated restriction of synthesis of the protein phosphatase 2A-A (PP2A-A).
PPP2R1A mutation is associated with endometrial carcinoma progression and abdominopelvic metastasis.
PPP2R1A mutations affect PP2A function and oncogenic signaling, illuminating the genetic basis for serous EC development.
PR65A phosphorylation regulates PP2A complex signaling.
Our results suggest that IH-induced ROS generation increases PP2A activation and subsequently downregulates ERK1/2 activation, which results in inhibition of PC12 cell proliferation through G0/G1 phase arrest and NGF-induced neuronal differentiation.
The two functional variants in PPP2R1A and PPP2R5E and their combinations are associated with lung cancer risk in the Chinese.
Partial unfolding of PR65/A impacts catalysis by altering the proximity of bound catalytic subunit and substrate.
For PPP2R1A, a heterozygous, somatic mutation (c.771G>T, p.W257C) was identified in 1 out of 37 patients (2.7%) with primary ovarian endometrioid carcinoma.
gene transcription of PPP2R1A regulated by the polymorphism and methylation in the promoter region
This study indicates that the PPP2R1A mutation occurs at a lower frequency compared to other gynecological malignancies, irrespective of the histological subtype
the frequent mutation of PPP2R1A in the serous type of uterine cancer, a low frequency of mutation in endometrioid endometrial cancer and absence of mutation in uterine carcinosarcoma.
Our findings suggest that functional genetic variants in the proximal promoter of the PP2A-Aalpha gene and their haplotypes are critical in the regulation of transcriptional activation.
identified somatic missense mutations in 40.8% of high-grade serous endometrial tumours and 5% of endometrial endometrioid carcinomas; mutations identified in ovarian tumours at lower frequencies;no mutations found in high- or low-grade serous carcinoma
PPP2R1A somatic mutations occur in certain types of uterine and ovarian neoplastic lesions, especially uterine serous carcinomas
PP2A-mediated dephosphorylation of Carma1 is a critical step to limit T-cell activation and effector cytokine production.
oocyte-specific deletion of Ppp2r1a led to severe female subfertility without affecting follicle survival, growth, and ovulation.
A Pak1-PP2A-ERM signaling axis mediates F-actin rearrangement and degranulation in mast cells.
PP2A (Protein Phosphatase 2A(Twins)) counteracts Plk4 autophosphorylation, thus stabilizing Plk4 and promoting centriole duplication
PP2A-A alpha transcriptional regulation is mediated by multiple factors including AP-2alpha, CREB, ETS-1, and SP-1
Data show that DSB promote PP2A to associate with Ku 70 and Ku 86.
protein phosphatase 2A overexpression in NIH 3T3 cells
T-cell receptor (TCR)-dependent tyrosine phosphorylation may be the mechanism by which the regulatory subunit of PP2A prevents the inhibitory function of CTLA-4, before TCR-CTLA-4 coligation.
PP-2A regulation of paxillin phosphorylation may have a role in controlling tumor cell adherence and motility.
PP2A may contribute to melanoma cell radioresistance: the truncated isoform of the PP2A B56gamma regulatory subunit reduces irradiation-induced Mdm2 phosphorylation
PP2A has a fundamental role in cardiac function
response of endothelial cells to the tumor-derived motility-stimulatory factors PGE2/TGFbeta involved a decline in the activity of PP2A, a loss of PP2A co-precipitation with PTEN, and an increase in the PTEN serine phosphorylation level.
heat treatment inactivates PP2A, which may subsequently cause ERK activation and decreases melanin synthesis in melanocytes
Results indicate that polyamines regulate protein phosphatase 2A (PP2A)activity, and inhibition of PP2A in response to polyamine depletion increases levels of Bad and Bcl-2 proteins and prevents cytochrome c release, caspase-9, and caspase-3 activation.
Pim on PP2A activity may mediate the levels of c-Myc and the phosphorylation of proteins needed for increased protein synthesis, which could have a significant impact on tumor growth
PP2A plays a positive rather than a negative role in the regulation of IKKbeta
the carboxy-terminal leucine L309 of the PP2A catalytic subunit determines PP2A heterotrimer composition in vivo. PP2A subunit composition plays a crucial role in regulating cell adhesion and as a consequence in the development of the Harderian gland.
PP2A-mediated dephosphorylation of BCL-2 is required to protect BCL-2 from proteasome-dependent degradation, affecting resistance to ER stress
p38alpha can negatively modulate Akt activity, independently of PI3K, by regulating the interaction between caveolin-1 and PP2A through a mechanism dependent on cell attachment.
PP2A is involved in the post-transcriptional regulation of tumor necrosis factor-alpha.
Akt dephosphorylation was mediated by ceramide-induced PKCzeta-Akt association and PP2A activation in Leishmania donovani-infected macrophages.
This gene encodes a constant regulatory subunit of protein phosphatase 2. 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 constant regulatory subunit A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. This gene encodes an alpha isoform of the constant regulatory subunit A. Alternatively spliced transcript variants have been described.
PP2A subunit A isoform PR65-alpha
, PP2A subunit A isoform R1-alpha
, medium tumor antigen-associated 61 KDA protein
, protein phosphatase 2 (formerly 2A), regulatory subunit A (PR 65), alpha isoform
, serine/threonine protein phosphatase 2A, 65 kDa regulatory subunit A, alpha isoform
, serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
, alpha isoform of regulatory subunit A, protein phosphatase 2
, protein phosphatase 2 (formerly 2A), regulatory subunit A, alpha isoform
, protein phosphatase 2 (formerly 2A), regulatory subunit A , alpha isoform
, protein phosphatase 2A 65 kDa regulatory subunit, alpha isoform
, protein phosphatase 2 (formerly 2A), regulatory subunit A, beta isoform
, medium tumor antigen-associated 61 kDa protein
, protein phosphatase 2, regulatory subunit A, alpha
, serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform-like
, protein phosphatase PP2A
, serine/threonine protein phosphatase A subunit type 2A
, protein phosphatase 2 regulatory subunit A, alpha S homeolog