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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.
These findings show that radiation induces S897 EphA2 phosphorylation, an event associated with increased cell survival. Therefore, targeting pathways that mediate EphA2 S897 phosphorylation may be a beneficial strategy to reduce radioresistance.
Our findings broaden the spectrum of causative mutations in EPHA2 gene for congenital cataract and suggest that WES is an efficient strategy to scan variants in known causative genes for genetically heterogeneous diseases.
Afadin (AFDN), a cytoskeletal and junction-associated protein, was present in 2D and 3D keratinocyte cultures, and validated as a so-far-unknown EphA2-interacting protein.
EphA2, a member of the large family of Ephrin receptor tyrosine kinases, is a functional signaling receptor for progranulin (show GRN Proteins).
EphA2 have the ability to negatively regulate the radiosensitivity of HCC (show FAM126A Proteins) 97H cells, which mainly depends on 38MAPK-mediated signal pathways.
both EphA2 and EphB4 (show EPHB4 Proteins) show potential as target for image-guided colorectal cancer surgery, but EphB4 (show EPHB4 Proteins) seems to have the best characteristics with respect to tumor/normal mucosa distribution
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 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 (show APOE Proteins)(-/-) mice.
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)