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Human PPP2CA Protein expressed in Wheat germ - ABIN1316010
Hung, Wang, Chen, Chu, Hsiao, Tai, Chao, Yu, Shiau, Chen: SET antagonist enhances the chemosensitivity of non-small cell lung cancer cells by reactivating protein phosphatase 2A. in Oncotarget 2016
PPP2CA may act as an oncogene in the progression of colorectal cancer
High PP2A expression is associated with Colorectal Cancer Cell Invasiveness.
PP2A overexpression is associated with lung metastasis in colorectal cancer .
Suspension survival mediated by PP2A-STAT3-Col XVII determines tumor initiation and metastasis in cancer stem cells.
alpha-Syn bound to PP2A Calpha by the hydrophobic interaction and upregulated its activity. Blocking the hydrophobic domain of alpha-Syn or hydrophilic mutation on the residue I123 in PP2A Calpha all reduced PP2A activity upregulation by alpha-Syn.
The results showed SNPs near PPP2CA were associated with decreased expression of PPP2CA mRNA in PBMCs from patients with SLE and suggested that the mRNA expression of the gene may be correlated with the pathogenesis of SLE.
This study demonstrated an association of PPP2CA (rs10491322 and rs7704116) with systemic lupus erythematosus susceptibility in a Chinese Han population. Furthermore, the minor allele of PPP2CA rs10491322 as a risk factor was correlated with immunologic disorders for systemic lupus erythematosus.
RAB9 competes with the catalytic subunit PPP2CA in binding to PPP2R1A. This competitive association has an important role in controlling the PP2A catalytic activity.
Results show that miR-199b is a tumor suppressor emerges as a potential contributing mechanism to inhibit PP2A via PP2A inhibitor SET (SET) overexpression in metastatic colorectal cancer (mCRC).
Data show that protein phosphatase-2A (PP2A) was upregulated in lung adenocarcinoma cell lines that were transfected with midline 1 E3 ubiquitin-protein ligase (MID1)-siRNA, suggesting MID1 negatively regulates PP2A in lung adenocarcinoma.
B55alpha-PP2A mutations in acute myeloid leukemia have roles in leukemogenesis by promoting AKT T308 phosphorylation and sensitivity to AKT inhibitor-induced growth arrest
This work has significantly advanced our understanding of the RACK1/PP2A complex and suggests a pro-carcinogenic role for the RACK1/PP2A interaction. This work suggests that approaches to target the RACK1/PP2A complex are a viable option to regulate PP2A activity and identifies a novel potential therapeutic target in the treatment of breast cancer.
Moreover, PP2Acalpha2-overexpressed cells demonstrated increased expression of IGBP1, activated mTORC1 signaling to reduce basal autophagy and increased anchorage-independent growth. Our study provides new insights into the complex mechanisms of PP2A regulation.
protein phosphatase 2A (PP2A)-mediated Raf-MEK-ERK signaling was involved in glutaminolysis in endothelial cells.
Studies indicate that protein phosphatase methylesterase-1 (PME-1) negatively regulates protein phosphatase 2A (PP2A) activity by highly complex mechanisms.
Binding of PP2A and Akt increased in response to cAMP or phosphatidic acid (PA), suggesting that their binding is directly responsible for the inactivation of Akt during decidualization.
Knockdown of Alpha4 preferentially impacts the expression of PP4c and PP6c compared to expression levels of PP2Ac.
these data support a role for the novel PP2Ac-CIN85 complex in supporting integrin-dependent platelet function by dampening the phosphatase activity.
PP2Ac upregulation has a poor prognostic impact on the overall survival of hepatocellular carcinoma (HCC) patients and contributes to the aggressiveness of HCC. PP2Ac may represent a potential therapeutic target for HCC.
Data show that downregulating proto-oncogene protein Akt (p-Akt) by inhibiting PP2A inhibitor SET-mediated protein phosphatase 2A (PP2A) inactivation determined the pro-apoptotic effects of EMQA and paclitaxel combination treatment.
PP2A Calpha in osteoblasts was also potentially involved in controlling adipocyte differentiation through a paracrine mechanism.
these data demonstrate that phosphatase PP2A is essential for TH17 differentiation and that inhibition of PP2A could be a possible therapeutic approach to controlling TH17-driven autoimmune diseases.
miR-203-3p target Ppp2ca aggravates status epilepticus model in mice.
Data (including data from studies in knockout/transgenic mice) suggest Ppp2ca supports cortical neuronal growth and cognitive function via regulating p73/Gls2 signal transduction in neurons of hippocampus. Ppp2ca gene knock-out results in embryonic cortical atrophy with learning/memory deficits. (Ppp2ca = protein phosphatase 2a catalytic subunit alpha isoform; p73 = transformation related protein 73; Gls2 = glutaminase-2)
Results indicate that Dlx5 and Runx2 are critical factors for the upregulated Osterix expression in shPP2A cells, which is considered to be important for the accelerated osteoblast differentiation in these cells.
Data (including data from studies in transgenic mice) suggest that Esr1 signaling promotes activation of Pp2a; here, central activation of Pp2a during estrogen replacement therapy is involved in prevention of menopause-induced obesity and glucose intolerance (that is, induced by lack of membrane-initiated Esr1 signaling). (Esr1 = estrogen receptor 1; Pp2a = protein phosphatase 2A)
The data also suggest that H2A.Z restricts transcription, which is moderated by ANP32e at the promoter and gene bodies of expressed genes. Thus, ANP32e, through inhibition of PP2A, is required for nucleosomal inclusion of H2A.Z and the regulation of gene expression
PP2A is a target of piperine, which induces autophagy in a rotenone-induced Parkinson's disease model
In vitro, SCF induced the phosphorylation of p38 MAPK and cofilin, leading to the migration of cardiac stem cells.
We describe a novel mechanism of signal transduction enriched in medium spiny neurons of striatum that likely mediates effects of the neurotransmitter dopamine acting on these cells. We find that the protein ARPP-16, which is highly expressed in striatal medium spiny neurons, acts as a selective inhibitor of certain forms of the serine/threonine protein phosphatase, PP2A, when phosphorylated by the kinase, MAST3.
data show that Fyn kinase is activated after TLR4 triggering and exerts an important negative control on LPS-dependent TNF production in mast cells controlling the inactivation of PP2Ac and activation of PKCalpha/beta necessary for the secretion of TNF by VAMP3(+) carriers
endogenous siRNA (PTEN-sh-3p21) cleaved from PTEN-sh within PTEN mRNA 3'UTR modulates PPP2CA and PTEN at the post-transcriptional level in liver cells
PP2A activation both limited and prevented inflammation and tissue injury in two direct injury models of Acute respiratory distress syndrome.
critical role in the proliferation and metastasis of osteosarcoma cells
PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte.
Study demonstrates that PPP2Ac-alpha plays important roles in both hair follicle and skin development.
these results suggest that inhibiting PP2Ac nitration using a mimic peptide is a potential preventive strategy for Endothelial-to-mesenchymal transition in renal fibrosis
Data suggest a critical role for the I2PP2A protein (SET)-protein phosphatase-2A (PP2A) signaling axis in Pten phosphohydrolase
that loss of glucocerebrosidase function may contribute to SNCA accumulation through inhibition of autophagy via PPP2A inactivation
Data indicate that protein phosphatase PP2A is required for the function of T(reg) cells and the prevention of autoimmunity.
changes in PP2A activity due to methylation and tyrosine phosphorylation occur in sperm; these changes may play an important role in the regulation of sperm function
The findings demonstrate an endothelial VEGF resistance mechanism conferred by palmitic acid, which comprises ceramide-induced, PP2A-mediated dephosphorylation of critical activation sites on enzymes central to vascular homeostasis and angiogenesis.
PP2A and AIP1 cooperatively induce activation of ASK1-JNK signaling and vascular endothelial cell apoptosis.
Hsp27 is dephosphorylated by PP2A in dorsal ruffles, in non-caveolar lipid raft microdomains.
This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A 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. This gene encodes an alpha isoform of the catalytic subunit.
, protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform
, protein phosphatase 2A catalytic subunit, alpha isoform
, replication protein C
, serine/threonine protein phosphatase 2A, catalytic subunit, alpha isoform
, serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
, protein phosphatase 2a, catalytic subunit, alpha isoform
, protein phosphatase 2, catalytic subunit, alpha isoform
, protein phosphatase-2A-alpha
, protein phosphatase 2A alpha subunit
, protein phosphatase 2 (formerly 2A), catalytic subunit, beta isoform
, type 2A protein phosphatase catalytic subunit
, protein phosphatase 2, catalytic subunit, beta isoform
, protein phosphatase 2, catalytic subunit, alpha isozyme
, serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform-like