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Human Polyclonal PTPRO Primary Antibody for IHC, IHC (p) - ABIN4348622
Zhang, Hou, Wang, Jiang, Yin, Ji, Deng, Huang, Wang, Sun: PTPRO-mediated autophagy prevents hepatosteatosis and tumorigenesis. in Oncotarget 2015
Using loss-of-function and gain-of-function approaches, we show that PTPRO promotes the formation of excitatory synapses
PTPROt thus functions as an obligate haploinsufficient TS in CLL, where its expression levels determine its role as a promoter or inhibitor of the tumorigenic process in mice. Partial loss of PTPROt generates the strongest disease phenotype, suggesting that its intermediate expression levels in CLL are selected for.
TLR4 and NF-kappaB/p65 phosphorylation was significantly enhanced in PTPRO over-expressing cells, while significantly down-regulated in PTPRO knockout cells. PTPRO plays ital roles in atherosclerosis (AS) via promoting ox-LDL induced oxidative stress and cell apoptosis through TLR4/NF-kappaB pathway.
PTPRO plays an important role in FH by interacting with TLR4.
Study show that EphA4 is a substrate for PTP-oc in osteoclasts and that the molecular mechanism contributing to the PTP-oc-induced up-regulation of the osteoclast activity in part involves its dephosphorylation and inactivation of the EphA4 signaling.
PTPRO truncated serves as an important tumor suppressor in hepatocellular carcinoma microenvironment.
The loss of PTPRO in the tumor niche was correlated with larger tumor volume, more metastases, increased number of circulating tumor cells, less apoptosis and reduced necrosis rates in the orthotopic mouse model of breast cancer.
PTPRO regulates insulin and lipid metabolism via the PI3K/Akt/MDM4/MDM2/P53 axis by affecting autophagy.
Survival and inflammation promotion effect of PTPRO in fulminant hepatitis is associated with NF-kappaB activation.
PTPRO deficiency resulted in reduction of NF-kappaB activation in both hepatocytes and macrophages and was correlated to c-Src phosphorylation.
PTPRO is expressed mainly in TrkB-expressing (TrkB(+)) and Ret(+) mechanoreceptors within the trigeminal ganglia during embryogenesis.
These results suggest that ptpro is a target gene of Wnt/beta-catenin signaling and that PTPRO may function as a novel receptor for Wnt.
Data indicate that PTPRO is required for peptidergic differentiation and process outgrowth of sensory neurons, as well as mature sensory function, and provide the first evidence that RPTPs regulate DRG development.
PTPRO might participate in regulation of dendritic morphology or synapse formation of interneurons in the adult mouse olfactory bulb
PTPRO is involved in the differentiation and axonogenesis of central and peripheral nervous system neurons, where it is in a position to modulate intracellular responses to neurotrophin-3 and/or nerve growth factor.
We find that at least one NPCD isoform is tyrosine phosphorylated in vivo and can serve as a substrate for PTPRO in vitro.
Ptpro moderates the amount of maximal activation of Eph receptors. In the chick retinotectal projection system, Ptpro controls the sensitivity of retinal axons to ephrins.
PTP-oc is a positive regulator of osteoclasts
the present study demonstrated that PTPRO inhibits tumor growth in vitro and in vivo, indicating the tumor suppressive function of PTPRO in LSCC. This study highlights PTPRO as an epigenetically silenced gene, and a candidate tumor-suppressor of LSCC.
Single nucleotide polymorphism in PTPRO gene is associated with Acute Renal Graft Rejection.
Results provide evidence that PTPRO inhibits ERBB2-driven breast cancer through dephosphorylation leading to dual effects of ERBB2 signaling suppression and endosomal internalization of ERBB2.
PTPRO is a novel candidate gene in emphysema with severe airflow obstruction.
These observations confirm that PTPRO plays a critical role in liver fibrogenesis by affecting PDGF signaling in HSC activation and might be developed into a feasible therapeutic approach for the treatment of chronic fibrotic liver diseases.
The optimal pH value of PTP-oc is approximately 7.0.
Loss of PTPRO expression is associated with chronic lymphocytic leukemia.
Results highlight the PTPRO contribution in negative regulation of SRC/EGFR signaling in colon cancer.
PTPRO was drastically decreased in fulminant hepatitis, and this was associated with enhanced beta-catenin accumulation but reduced IFN-gamma secretion.
Our study suggests an interesting PTPRO/TLR4/NF-kappaB signaling feedback loop in Hhepatocellular carcinomcarcinogenesis and progression
PTPRO level was decreased in the early phase but reversed in the late phase of hepatic ischemia reperfusion injury.
PTPRO methylation is associated with poor survival only in HER2-positive patients.
methylation and downregulation of PTPRO in a subset of primary human HCC and establish VCP as a novel functionally important substrate of this tyrosine phosphatase that could be a potential molecular target for HCC therapy.
ErbB2 is a direct substrate of PTPRO and decreased expression of PTPRO predicts poor prognosis for ErbB2-positive breast cancer patients.
Three intronic SNPs in PTPRO were associated with learning and memory.
hypermethylated PTPRO occurs frequently in esophageal squamous cell carcinoma
These findings further substantiate the role of TCL1 in PTPROt suppression and its importance in the pathogenesis of chronic lymphocytic leukemia.
The present study introduces mutations in PTPRO as another cause of autosomal-recessive nephrotic syndrome.
conclude that an intronic promoter within the protein tyrosine phosphatase, receptor type(GLEPP1) gene drives the expression of the protein tyrosine phosphatase-osteoclast(PTP) in a cell type-specific manner
This gene encodes a member of the R3 subtype family of receptor-type protein tyrosine phosphatases. These proteins are localized to the apical surface of polarized cells and may have tissue-specific functions through activation of Src family kinases. This gene contains two distinct promoters, and alternatively spliced transcript variants encoding multiple isoforms have been observed. The encoded proteins may have multiple isoform-specific and tissue-specific functions, including the regulation of osteoclast production and activity, inhibition of cell proliferation and facilitation of apoptosis. This gene is a candidate tumor suppressor, and decreased expression of this gene has been observed in several types of cancer.
glomerular epithelial protein 1
, osteoclastic phosphotyrosyl phosphatase
, Glomerular epithelial protein 1
, receptor-type protein tyrosine phosphatase D30
, receptor-type tyrosine-protein phosphatase O
, PTPase U2
, protein tyrosine phosphatase U2
, protein tyrosine phosphatase, non-receptor type 15
, receptor protein tyrosine phosphatase RO
, PTP phi
, osteoclastic transmembrane protein-tyrosine phosphatase
, phosphotyrosine phosphatase U2
, protein tyrosine phosphatase PTP-U2