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anti-Human EPH Receptor A2 Antibodies:
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Human Polyclonal EPH Receptor A2 Primary Antibody for 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. in PLoS ONE 2011
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Human Monoclonal EPH Receptor A2 Primary Antibody for 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. in PLoS ONE 2015
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Mouse (Murine) Monoclonal EPH Receptor A2 Primary Antibody for 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. in 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 for IHC, ELISA - ABIN1724651
Landen, Kinch, Sood: EphA2 as a target for ovarian cancer therapy. in Expert opinion on therapeutic targets 2005
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Human Monoclonal EPH Receptor A2 Primary Antibody for IHC (p), ELISA - ABIN533530
Nakamoto, Bergemann: Diverse roles for the Eph family of receptor tyrosine kinases in carcinogenesis. in Microscopy research and technique 2002
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Human Polyclonal EPH Receptor A2 Primary Antibody for IF (p), IHC (p) - ABIN669201
Wu, Fu, Zhou, Gong, Liu, Qiao, Li: HIF-1? and HIF-2?: siblings in promoting angiogenesis of residual hepatocellular carcinoma after high-intensity focused ultrasound ablation. in PLoS ONE 2014
Human Monoclonal EPH Receptor A2 Primary Antibody for 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. in 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 for IHC (p), WB - ABIN3044136
Yang, Min: Effect of ephrin-A1/EphA2 on invasion of trophoblastic cells. in 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
Human Monoclonal EPH Receptor A2 Primary Antibody for 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. in Cell stem cell 2017
Human Monoclonal EPH Receptor A2 Primary Antibody for 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. in Cancer research 2017
Data show that interleukin 1 receptor associated kinase 4 (IRAK4) and EPH receptor A2 (EphA2) were the functional targets of miR-302b.
The C (minor) allele decreased EPHA2 transcriptional activity relative to the T allele by reducing the binding affinity of PAX2 to the EPHA2 promoter region.
We have identified a recurrent splice-site mutation c.2826-9G>A in EPHA2 causing isolated posterior nuclear cataract, providing evidence of further phenotypic heterogeneity associated with this variant.
Our study demonstrated that EphA2 rescued by miR-124 downregulation conferred the erlotinib resistance of pancreatic cancer cell Capan-1 with K-RAS mutation.
We created a novel pH-dependent transmembrane peptide, TYPE7, by altering the sequence of the transmembrane domain of EphA2..TYPE7 binds to endogenous EphA2 and reduces Akt phosphorylation and cell migration as effectively as ephrinA1
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.
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.
Here, the authors systematically investigated the bindings of each SAM domain of Eph receptors to the SAM domains from SHIP2 and Odin, and uncover a highly specific SAM-SAM interaction-mediated cytoplasmic Eph-effector binding pattern.
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.
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.
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
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)