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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
PP2A (show PPP2R4 Proteins) overexpression is associated with lung metastasis in colorectal cancer .
Suspension survival mediated by PP2A (show PPP2R4 Proteins)-STAT3 (show STAT3 Proteins)-Col (show HDAC1 Proteins) XVII determines tumor initiation and metastasis in cancer stem cells.
alpha-Syn bound to PP2A (show PPP2R4 Proteins) Calpha (show PRKACA Proteins) by the hydrophobic interaction and upregulated its activity. Blocking the hydrophobic domain of alpha-Syn or hydrophilic mutation on the residue I123 in PP2A (show PPP2R4 Proteins) Calpha (show PRKACA Proteins) all reduced PP2A (show PPP2R4 Proteins) 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 (show RAB9A Proteins) competes with the catalytic subunit PPP2CA in binding to PPP2R1A (show PPP2R1A Proteins). This competitive association has an important role in controlling the PP2A (show PPP2R4 Proteins) catalytic activity.
Results show that miR (show MLXIP Proteins)-199b is a tumor suppressor emerges as a potential contributing mechanism to inhibit PP2A (show PPP2R4 Proteins) via PP2A (show PPP2R4 Proteins) inhibitor SET (SET) overexpression in metastatic colorectal cancer (mCRC).
Data show that protein phosphatase-2A (PP2A (show PPP2R4 Proteins)) was upregulated in lung adenocarcinoma cell lines that were transfected with midline 1 (show MID1 Proteins) E3 ubiquitin-protein ligase (show UBE2K Proteins) (MID1 (show MID1 Proteins))-siRNA, suggesting MID1 (show MID1 Proteins) negatively regulates PP2A (show PPP2R4 Proteins) in lung adenocarcinoma.
B55alpha (show PPP2R2A Proteins)-PP2A (show PPP2R4 Proteins) mutations in acute myeloid leukemia (show BCL11A Proteins) have roles in leukemogenesis by promoting AKT (show AKT1 Proteins) T308 phosphorylation and sensitivity to AKT (show AKT1 Proteins) inhibitor-induced growth arrest
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.
Results indicate that Dlx5 (show DLX5 Proteins) and Runx2 (show RUNX2 Proteins) are critical factors for the upregulated Osterix (show SP7 Proteins) 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 (show H2AFZ Proteins) restricts transcription, which is moderated by ANP32e (show ANP32E Proteins) at the promoter and gene bodies of expressed genes. Thus, ANP32e (show ANP32E Proteins), through inhibition of PP2A (show PPP2R2B Proteins), is required for nucleosomal inclusion of H2A.Z (show H2AFZ Proteins) and the regulation of gene expression
PP2A (show PPP2R2B Proteins) is a target of piperine, which induces autophagy in a rotenone-induced Parkinson's disease model
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.
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
, 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