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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
In vitro, SCF (show KITLG Proteins) induced the phosphorylation of p38 MAPK (show MAPK14 Proteins) and cofilin (show CFL1 Proteins), 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 (show FYN Proteins) kinase is activated after TLR4 (show TLR4 Proteins) triggering and exerts an important negative control on LPS (show TLR4 Proteins)-dependent TNF (show TNF Proteins) production in mast cells controlling the inactivation of PP2Ac and activation of PKCalpha (show PKCa Proteins)/beta necessary for the secretion of TNF (show TNF Proteins) by VAMP3 (show VAMP3 Proteins)(+) 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 (show PPP2R2B Proteins) activation both limited and prevented inflammation and tissue injury in two direct injury models of Acute respiratory distress syndrome.
PP2A (show PPP2R2B Proteins) regulates kinetochore-microtubule attachment during meiosis I in oocyte.
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 (show KCNH2 Proteins)) cells and the prevention of autoimmunity.
This work has significantly advanced our understanding of the RACK1 (show GNB2L1 Proteins)/PP2A (show PPP2R4 Proteins) complex and suggests a pro-carcinogenic role for the RACK1 (show GNB2L1 Proteins)/PP2A (show PPP2R4 Proteins) interaction. This work suggests that approaches to target the RACK1 (show GNB2L1 Proteins)/PP2A (show PPP2R4 Proteins) complex are a viable option to regulate PP2A (show PPP2R4 Proteins) activity and identifies a novel potential therapeutic target in the treatment of breast cancer.
Moreover, PP2Acalpha2-overexpressed cells demonstrated increased expression of IGBP1 (show IGBP1 Proteins), activated mTORC1 signaling to reduce basal autophagy and increased anchorage-independent growth. Our study provides new insights into the complex mechanisms of PP2A (show PPP2R4 Proteins) regulation.
protein phosphatase 2A (PP2A (show PPP2R4 Proteins))-mediated Raf (show RAF1 Proteins)-MEK (show MAP2K1 Proteins)-ERK (show EPHB2 Proteins) signaling was involved in glutaminolysis in endothelial cells.
Studies indicate that protein phosphatase methylesterase-1 (PME-1 (show PPME1 Proteins)) negatively regulates protein phosphatase 2A (PP2A (show PPP2R4 Proteins)) activity by highly complex mechanisms.
Binding of PP2A (show PPP2R4 Proteins) and Akt (show AKT1 Proteins) increased in response to cAMP or phosphatidic acid (PA), suggesting that their binding is directly responsible for the inactivation of Akt (show AKT1 Proteins) during decidualization.
Knockdown of Alpha4 preferentially impacts the expression of PP4c (show PPP4C Proteins) and PP6c (show PPP6C Proteins) compared to expression levels of PP2Ac.
these data support a role for the novel PP2Ac-CIN85 (show SH3KBP1 Proteins) 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 (show FAM126A Proteins)) patients and contributes to the aggressiveness of HCC (show FAM126A Proteins). PP2Ac may represent a potential therapeutic target for HCC (show FAM126A Proteins).
Data show that downregulating proto-oncogene (show RAB1A Proteins) protein Akt (p-Akt (show AKT1 Proteins)) by inhibiting PP2A (show PPP2R4 Proteins) inhibitor SET-mediated protein phosphatase 2A (PP2A (show PPP2R4 Proteins)) inactivation determined the pro-apoptotic effects of EMQA and paclitaxel combination treatment.
Data suggest a critical role for the I2PP2A protein (SET)-protein phosphatase-2A (PP2A) signaling axis in Pten protein (Pten) deficient castration resistant prostate cancer (CRPC) progression.
changes in PP2A (show PPP2R2B Proteins) 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 (show VEGFA Proteins) resistance mechanism conferred by palmitic acid, which comprises ceramide-induced, PP2A (show PPP2R2B Proteins)-mediated dephosphorylation of critical activation sites on enzymes central to vascular homeostasis and angiogenesis.
PP2A (show PPP2R2B Proteins) and AIP1 (show PDCD6IP Proteins) cooperatively induce activation of ASK1 (show MAP3K5 Proteins)-JNK (show MAPK8 Proteins) signaling and vascular endothelial cell apoptosis.
Hsp27 (show HSPB1 Proteins) is dephosphorylated by PP2A (show PPP2R2B Proteins) 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
, serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
, protein phosphatase 2a, catalytic subunit, alpha
, protein phosphatase 2 (formerly 2A), catalytic subunit, beta isoform
, protein phosphatase 2, catalytic subunit, beta isoform
, protein phosphatase 2, catalytic subunit, alpha isozyme
, serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform-like
, protein phosphatase 2a, catalytic subunit, alpha isoform
, protein phosphatase 2A catalytic subunit, alpha isoform
, replication protein C
, serine/threonine protein phosphatase 2A, catalytic subunit, alpha isoform
, protein phosphatase 2, catalytic subunit, alpha isoform
, protein phosphatase-2A-alpha
, type 2A protein phosphatase catalytic subunit
, protein phosphatase 2A alpha subunit
, phosphatase 2A catalytic subunit