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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 ELISA Kits) kinase is activated after TLR4 (show TLR4 ELISA Kits) triggering and exerts an important negative control on LPS (show TLR4 ELISA Kits)-dependent TNF (show TNF ELISA Kits) production in mast cells controlling the inactivation of PP2Ac and activation of PKCalpha (show PKCa ELISA Kits)/beta necessary for the secretion of TNF (show TNF ELISA Kits) by VAMP3 (show VAMP3 ELISA Kits)(+) 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.
PP2A 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 ELISA Kits)) cells and the prevention of autoimmunity.
data identify a molecular mechanism linking PP2A to the development of AD-related cognitive impairments that might be therapeutically exploited to target selectively the pathological effects caused by elevated Abeta (show APP ELISA Kits) levels in AD patients
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 (show PPP2R4 ELISA Kits))-mediated Raf (show RAF1 ELISA Kits)-MEK (show MAP2K1 ELISA Kits)-ERK (show EPHB2 ELISA Kits) signaling was involved in glutaminolysis in endothelial cells.
Studies indicate that protein phosphatase methylesterase-1 (PME-1 (show PPME1 ELISA Kits)) negatively regulates protein phosphatase 2A (PP2A (show PPP2R4 ELISA Kits)) activity by highly complex mechanisms.
Binding of PP2A (show PPP2R4 ELISA Kits) and Akt (show AKT1 ELISA Kits) increased in response to cAMP or phosphatidic acid (PA), suggesting that their binding is directly responsible for the inactivation of Akt (show AKT1 ELISA Kits) during decidualization.
Knockdown of Alpha4 preferentially impacts the expression of PP4c (show PPP4C ELISA Kits) and PP6c (show PPP6C ELISA Kits) compared to expression levels of PP2Ac.
these data support a role for the novel PP2Ac-CIN85 (show SH3KBP1 ELISA Kits) 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 ELISA Kits)) patients and contributes to the aggressiveness of HCC (show FAM126A ELISA Kits). PP2Ac may represent a potential therapeutic target for HCC (show FAM126A ELISA Kits).
Data show that downregulating proto-oncogene (show RAB1A ELISA Kits) protein Akt (p-Akt (show AKT1 ELISA Kits)) by inhibiting PP2A (show PPP2R4 ELISA Kits) inhibitor SET-mediated protein phosphatase 2A (PP2A (show PPP2R4 ELISA Kits)) 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 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 (show PDCD6IP ELISA Kits) cooperatively induce activation of ASK1 (show MAP3K5 ELISA Kits)-JNK (show MAPK8 ELISA Kits) 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
, 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