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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
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.
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 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