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These observations demonstrate that EphA2 affects the sensitivity to oxaliplatin by inducing EMT (show ITK Proteins) in oxaliplatin-resistant gastric cancer cells.
High erythropoietin (show EPO Proteins)-producing hepatocellular carcinoma receptor A (EphA) 1 (show EPHA1 Proteins), 2, and 4 expression levels were significantly related to recurrence.
Data show that Ephrin B3 (show EFNB3 Proteins) was concomitantly expressed with EphA2 and Ephrin A1 (show EFNA1 Proteins) with higher Ephrin B3 (show EFNB3 Proteins) 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.
data suggest that novel germ-line (blood) and somatic (lens) coding SNVs in EPHA2 that are predicted to be functionally deleterious occur in adults over 50 years of age
The YSA peptide stabilizes the EphA2 dimer.
A 3D structural model of a mutant with a novel 39-AA polypeptide at the C-terminus had partial disorder in the acquired C-terminal tail and a few residues making an alpha-helix and 2 short beta-strands. 2 peptides comprising the whole C-terminus and its predicted helical region, respectively, did not interact with EphA2-Sam (show TTN Proteins) or Ship2 (show INPPL1 Proteins)-Sam (show TTN Proteins). The C-terminus should not wrap the EphA2-Sam (show TTN Proteins) End-Helix interface or affect Sam (show TTN Proteins) dom (show SOX10 Proteins)...
EphA2 expression is enriched in the basal-like breast cancer molecular subtype and correlates with poor recurrence-free survival in human triple-negative breast cancers
The SAM (show TTN Proteins) domain inhibits EphA2-ligands interactions in the plasma membrane.
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.
Collectively, these data suggest that ATRA attenuates bleomycin-induced pulmonary fibrosis by regulating EphA2-EphrinA1 and PI3K-Akt (show AKT1 Proteins) 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 (show EFNA2 Proteins) and ephrin-A5 (show EFNA5 Proteins) 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 (show SLIT2 Proteins) by EphA2 receptor regulates endothelial responses to VEGF (show VEGFA Proteins)-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.
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)