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Human EZR Protein expressed in Human - ABIN2720647
Miyaji, Shahrizaila, Umapathi, Chan, Hirata, Yuki: Are ERM (ezrin/radixin/moesin) proteins targets for autoantibodies in demyelinating neuropathies? in Human immunology 2015
Show all 2 references for ABIN2720647
The present study showed over-expression of ezrin and moesin (show MSN Proteins) in colorectal carcinoma
study indicates that the presence of autoantibodies against Ezrin is significantly associated with ESCC
Ezrin protein is highly expressed in human PHC (show SLC25A3 Proteins) tissue which can be used for the prediction of metastasis disease.
results show that the activation of the ezrin-pAkt signaling axis is associated with the more aggressive clinicopathological features of PPA compared with LPA
Ezrin and p65 (show GORASP1 Proteins) interactions in MDA-MB-231 cells were confirmed using co-immunoprecipitation.
the distribution of NHERF1 (show SLC9A3R1 Proteins) in ovarian cancer and reveals a different regulation of NHERF1 (show SLC9A3R1 Proteins) and EZRIN expression in ovarian tumors which represents the complexity of the molecular changes of this disease
Phosphorylation of ezrin together with its binding to phosphatidylinositol-4,5-bisphosphate tethers the F508del CFTR to the actin cytoskeleton, stabilizing it on the apical membrane and rescuing the sub-membrane compartmentalization of cAMP and activated PKA.
Data show that gene silence of ezrin inhibits the proliferation and invasion of prostate cancer PC-3 (show PCSK1 Proteins) cells, meanwhile the level of E-cadherin (show CDH1 Proteins) is upregulated and N-cadherin (show CDH2 Proteins) is downregulated.
Knockdown of ezrin in HUVECs significantly induced the morphogenetic changes and cytoskeletal reorganization of the transfected cells, and also reduced cell migration and angiogenesis capacity in vitro.
High EZRIN expression is associated with prostate cancer.
Ezrin and CK18 (show KRT18 Proteins) are downregulated during implantation in cattle. The expression changes represent a temporal depolarization, which could be important for an establishment of bovine pregnancy.
Ezrin-dependent, membrane-specific translocation and activation of calpain by VEGF (show VEGFA Proteins) precedes AMPK (show PRKAA1 Proteins) and AKT (show AKT1 Proteins)-dependent phosphorylation of eNOSs1179 and production of NO.
Ezrin may play a role in regulating lymphatic metastasis in hepatocellular carcinoma and might be inversely associated with A7 expression.
Augmented hypertension-induced glomerular capillary injury in mice lacking CLIC5 results from abrogation of Rac1-dependent Pak and ezrin activation, perhaps reducing the tensile strength of the podocyte actin cytoskeleton.
Data, including data from studies in knockout mice, suggest that VDR (vitamin D receptor) regulates expression of ezrin in enterocytes; VDR (show CYP27B1 Proteins) appears not to be involved in morphology of tight junctions and absorption of large molecules in enterocytes.
Lack of ezrin not only causes achlorhydria and hypergastrinemia but also changes the structure of gastric glands, with severe perturbation of the secretory membranes of parietal cells.
our study demonstrates that ezrin is a novel regulator of IL-10 (show IL10 Proteins) production by B cells
Merlin (show NF2 Proteins) and Ezrin are components of a mechanism where mechanical forces associated with cell junctions are transduced across the cell cortex via cortical actomyosin cytoskeleton to control lateral mobility and activity of epidermal growth factor receptor (show EGFR Proteins).
Dysfunction of ezrin mimics important aspects of the pathological mechanisms responsible for cholangiopathies
We hypothesize that polyvalent electrostatic interactions are responsible for the assembly of CD44 (show CD44 Proteins) clusters and the multimeric PIP2-CD44 (show CD44 Proteins)-Ezrin complexes.
These results indicate that ezrin is required for uptake of hypotaurine from maternal serum by placental trophoblasts, and plays an important role in fetal growth.
These data altogether suggest a novel role of ezrin in the neuritogenesis of the cultured cortical neurons through down-regulation of RhoA (show RHOA Proteins) activity.
The cytoskeletal linker protein (show LAT Proteins) ezrin plays a significant role in hypothermic preservation injury in renal epithelia.
Coexpression of ezrin with Eps8 promotes the formation of membrane ruffles and tufts of microvilli, whereas expression of ezrin and Eps8L1a induces the clustering of actin-containing structures at the cell surface.
These findings reveal that direct ezrin interactions promote PTH1R apical localization and signaling in LLC-PK1 cells.
Spatial control of proton pump H,K-ATPase (show ATP1A1 Proteins) docking at the apical membrane by phosphorylation-coupled ezrin-syntaxin 3 (show STX3 Proteins) interaction.
1) NHE3 (show SLC9A3 Proteins) basal activity is regulated by a signaling complex that is controlled by sequential effects of two kinases, Akt (show AKT1 Proteins) and GSK-3, which act on a Ser (show SIGLEC1 Proteins) cluster in the same NHE3 (show SLC9A3 Proteins) C-terminal domain that binds ezrin
Ezrin-mediated F-actin interaction with the epithelial cell may direct membrane recruitment and cytoskeletal surface extension.
relatively high turnover of ezrin T567 phosphorylation was observed in all three epithelia (gastric, kidney and intestine).
VLN2 and VLN3 act redundantly in sclerenchyma development via bundling of actin filaments.
Data indicate that the construction of actin collars was affected in vln2 vln5 double mutantpollen tubes.
VLN2 and VLN3 play a role in actin filament organization in Arabidopsis.
The cytoplasmic peripheral membrane protein encoded by this gene functions as a protein-tyrosine kinase substrate in microvilli. As a member of the ERM protein family, this protein serves as an intermediate between the plasma membrane and the actin cytoskeleton. This protein plays a key role in cell surface structure adhesion, migration and organization, and it has been implicated in various human cancers. A pseudogene located on chromosome 3 has been identified for this gene. Alternatively spliced variants have also been described for this gene.
, villin 2 (ezrin)
, cytovillin 2