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anti-Human EPH Receptor A2 Anticorps:
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Human Polyclonal EPH Receptor A2 Primary Antibody pour CyTOF, FACS - ABIN4899913
Gopal, Bohonowych, Lema-Tome, Liu, Garrett-Mayer, Wang, Isaacs: A novel extracellular Hsp90 mediated co-receptor function for LRP1 regulates EphA2 dependent glioblastoma cell invasion. dans PLoS ONE 2011
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Human Monoclonal EPH Receptor A2 Primary Antibody pour CyTOF, FACS - ABIN4899912
Liao-Chan, Daine-Matsuoka, Heald, Wong, Lin, Cai, Lai, DAlessio, Theunissen: Quantitative assessment of antibody internalization with novel monoclonal antibodies against Alexa fluorophores. dans PLoS ONE 2015
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Mouse (Murine) Monoclonal EPH Receptor A2 Primary Antibody pour CyTOF, FACS - ABIN4899679
De Robertis, Loiacono, Fusilli, Poeta, Mazza, Sanchez, Marchionni, Signori, Lamorte, Vescovi, Garcia-Foncillas, Fazio: Dysregulation of EGFR Pathway in EphA2 Cell Subpopulation Significantly Associates with Poor Prognosis in Colorectal Cancer. dans Clinical cancer research : an official journal of the American Association for Cancer Research 2016
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Human Monoclonal EPH Receptor A2 Primary Antibody pour IHC, ELISA - ABIN1724651
Landen, Kinch, Sood: EphA2 as a target for ovarian cancer therapy. dans Expert opinion on therapeutic targets 2005
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Human Monoclonal EPH Receptor A2 Primary Antibody pour IHC (p), ELISA - ABIN533530
Nakamoto, Bergemann: Diverse roles for the Eph family of receptor tyrosine kinases in carcinogenesis. dans Microscopy research and technique 2002
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Human Monoclonal EPH Receptor A2 Primary Antibody pour FACS - ABIN4896889
Udyavar, Wooten, Hoeksema, Bansal, Califano, Estrada, Schnell, Irish, Massion, Quaranta: Novel Hybrid Phenotype Revealed in Small Cell Lung Cancer by a Transcription Factor Network Model That Can Explain Tumor Heterogeneity. dans Cancer research 2017
Human Monoclonal EPH Receptor A2 Primary Antibody pour FACS - ABIN4896891
Haas, Sciuto, Brunetto, Valvo, Signore, Fiori, di Martino, Giannetti, Morgante, Boe, Patrizii, Warnken, Schnölzer, Ciolfi, Di Stefano, Biffoni, Ricci-Vitiani, Pallini, De Maria: Integrin α7 Is a Functional Marker and Potential Therapeutic Target in Glioblastoma. dans Cell stem cell 2017
Human Polyclonal EPH Receptor A2 Primary Antibody pour FACS, IHC (p) - ABIN391885
Lindberg, Hunter: cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. dans Molecular and cellular biology 1991
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Human Monoclonal EPH Receptor A2 Primary Antibody pour IHC, ELISA - ABIN966072
Abraham, Knapp, Cheng, Snyder, Mittal, Bangari, Kinch, Wu, Dhariwal, Mohammed: Expression of EphA2 and Ephrin A-1 in carcinoma of the urinary bladder. dans Clinical cancer research : an official journal of the American Association for Cancer Research 2006
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Human Polyclonal EPH Receptor A2 Primary Antibody pour IHC (p), WB - ABIN3044136
Yang, Min: Effect of ephrin-A1/EphA2 on invasion of trophoblastic cells. dans Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban 2011
High EPHA2 expression is associated with metastatic onset of Ewing sarcoma.
miR-124-3p inhibits glioma cell proliferation. miR-124-3p inhibits glioma cell motility. miR-124-3p was found to suppress the growth, migration and invasion of glioma cells in vitro via EphA2. EphA2 is a candidate target of miR-124-3p.
Plasmodium sporozoites can invade hepatocytic cells independently of the Ephrin receptor A2
Binding of Candida albicans to ephrin type-A receptor 2 (EphA2) on oral epithelial cells activates signal transducer and activator of transcription 3 and mitogen-activated protein kinase signalling, and is required for induction of a proinflammatory and antifungal response. EphA2 (-/-) mice have impaired inflammatory responses and reduced interleukin-17 signalling during oropharyngeal candidiasis.
EphA2 has a role in extracellular vesicle secretion from senescent cells that promote cancer cell proliferation
Combination of polymorphisms in the NOD2, IL17RA, EPHA2 and KALRN genes could play a significant role in the development of sarcoidosis by maintaining a chronic pro-inflammatory status in macrophages
Phosphorylation of RCP at Ser(435) by Lemur tyrosine kinase-3 (LMTK3) and of EphA2 at Ser(897) by Akt are both necessary to promote Rab14-dependent (and Rab11-independent) trafficking of EphA2 which generates cell:cell repulsion events that drive tumour cells apart.
EphA2 SAM domain inhibits kinase activity by reducing receptor oligomerization.
miR-141 inhibits glioma neovascularization by controlling EphA2 expression.
when overexpressed, EphA2 induces ERK activation through its tyrosine kinase activity, leading to S897 phosphorylation and promotion of glioblastoma cell proliferation.
findings suggested inhibition of HDACs-EphA2 signaling axis with WW437 alone or in combination with other agents may be a promising therapeutic strategy for advanced breast cancer.
High EPHA2 expression is associated with epithelial-mesenchymal transition in gastric cancer.
Ligand-independent activation of EphA2 was triggered by VEGF released from CAF-CM.
EphA2-mediates glutaminolysis through YAP/TAZ activation in HER2-positive breast cancer and may serve as potential therapeutic targets in patients.
Data indicate a promising role for EPH receptor A2 (EPHA2) as a target in antibody treatments for melanoma.
These observations demonstrate that EphA2 affects the sensitivity to oxaliplatin by inducing EMT in oxaliplatin-resistant gastric cancer cells.
High erythropoietin-producing hepatocellular carcinoma receptor A (EphA) 1, 2, and 4 expression levels were significantly related to recurrence.
Data show that Ephrin B3 was concomitantly expressed with EphA2 and Ephrin A1 with higher Ephrin B3 levels found in non-squamous than in squamous tumors.
These results suggest that EphA2/Efna1/Egfr genes, linked to a possible control by miR-200a and miR-26b, could be proposed as novel CRC prognostic biomarkers. Moreover, EphA2 could be linked to a mechanism of resistance to cetuximab alternative to KRAS mutations.
the dimer structures of human EphA2 receptor depend on the lipid environment, which we show is linked to the location of the structural motifs in the dimer interface, thereby establishing that both sequence and membrane composition modulate the complete energy landscape of membrane-bound proteins.
The present study successfully assessed the expression pattern of miR26b in the pituitary tissue of Yanbian cattle, and also confirmed that EphA2 was a target gene of miR26b in Yanbian cattle in vitro.
that Epha2 and Efna5 participate in the complex, global patterning of lens fiber cells that is necessary for maximal optical quality
EphA2 mAb treatment could partially inhibit LPSinduced inactivation of EphBEphrin B3 signalling, while Ephrin B3 overexpression could abrogate LPSinduced activation of EphA2Ephrin A1 signalling. EphB1/Ephrin B3 signalling may antagonise the EphA2/Ephrin A1dependent pathway following LPS treatment.
Whilst the EphA/ephrinA system may therefore play a role in the development of innervation of the cochlea and neural circuitry of the auditory brainstem, there appears to be a functional redundancy between members of this family such that loss of ephrinA2 function alone is insufficient to alter auditory function in the mouse.
Collectively, these data suggest that ATRA attenuates bleomycin-induced pulmonary fibrosis by regulating EphA2-EphrinA1 and PI3K-Akt signaling.
Lipopolysaccharide exposure significantly up-regulated EphA2 and EphrinA1 expression.
modulation of EphA2 signaling might contribute to effective transplantation of tissue-specific resident macrophages and/or monocytes
Our data suggest that EphA2 is closely related to the formation of osteoblasts and resorption of osteoclast and is likely to play an role in bone resorption induced in chronic periodontitis
We examined the roles of ephrin-A2 and ephrin-A5 signaling in contralateral targeting and topographic ordering in the ventral cochlear nucleus
EphA2 acts as a KRas cooperative tumor suppressor
Data shows that modulation of angiostatic factor Slit2 by EphA2 receptor regulates endothelial responses to VEGF-mediated angiogenesis and tumor neovascularization.
Sporozoites productively infected hepatocytes with high EphA2 expression, and the deletion of EphA2 protected mice from liver infection.
EphA2-mutant mice are more prone to hyperglycemia-induced increased injury and decreased survival.
EphA2 receptor silencing attenuates the extent and inflammation of atherosclerotic lesions in ApoE(-/-) mice.
these data demonstrate a role for EPHA2 in the maintenance and progression of NSCLCs and provide evidence that ALW-II-41-27 effectively inhibits EPHA2-mediated tumor growth in preclinical models of NSCLC.
These results indicate that EphA2/Src signaling is essential for the formation of the lens fulcrum. EphA2 also regulates Src/cortactin/F-actin complexes at the vertices of hexagonal equatorial cells for cell-to-cell alignment.
The EphA2 receptor directly contributes to blood-brain barrier damage and neuronal death following ischemic stroke.
results identify EphA2, a tyrosine kinase with known functions in neovascularization and oncogenesis, as an entry receptor for Kaposi's sarcoma-associated herpesvirus
In early bleomycin injury in WT mice, the expression of both EphA2 and ephrin-A1 increased.
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. Mutations in this gene are the cause of certain genetically-related cataract disorders.
ephrin type-A receptor 2
, epithelial cell receptor protein tyrosine kinase
, soluble EPHA2 variant 1
, tyrosine-protein kinase receptor ECK
, ephrin receptor EphA2
, epoxide hydrolase
, EPH receptor A2
, epithelial cell kinase
, tyrosine-protein kinase receptor MPK-5
, tyrosine-protein kinase receptor SEK-2
, protein tyrosine kinase EphA2
, eph-like receptor tyrosine kinase 6
, EPH receptor A2 L homeolog
, ephrin receptor EphA2 (tyrosine kinase family)