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Mouse (Murine) EPH Receptor A2 ELISA Kit for Sandwich ELISA - ABIN814270
Park, Choi, Choi, Yim, Roh: High Doses of Caffeine during the Peripubertal Period in the Rat Impair the Growth and Function of the Testis. in International journal of endocrinology 2015
Data show that the EphA2 ectodomain harbors a membrane-binding motif in the FN2 (show FN1 ELISA Kits) domain which preferentially interacts with anionic lipids.
Data show that microRNA miR (show MLXIP ELISA Kits)-141 is down-regulated in hepatocellular carcinoma (HCC (show FAM126A ELISA Kits)) tissues and it is negatively correlated with erythropoietin (show EPO ELISA Kits)-producing hepatocellular receptor A2 (EphA2) expression.
Nuclear expression of EphA2 in this series of large tumours was significantly associated with an increased rate of metastasis. On the other hand, cytoplasmic localisation was associated with a better prognosis. As there was no correlation between EphA2 expression and angiogenesis, the mature vasculature or VM, EphA2 appears to become less important in the advanced stages of the disease.
These data suggest that miR (show MLXIP ELISA Kits)-26b enhances the radiosensitivity of 97H hepatocellular cancer cells by targeting EphA2 protein.
EphA2 protein may be used as a new marker for the prognosis of clear cell renal cell carcinoma.
Mis (show AMH ELISA Kits)-localization of two of the mutant proteins in epithelial cells suggests that some disease-causing mutations in EPHA2 likely affect lens epithelial cell homeostasis and contribute to cataract.
EphA2 Expression Is a Key Driver of Migration and Invasion and a Poor Prognostic Marker in Colorectal Cancer
Based on these findings we propose that EphA2 promotes cell adhesion by an unknown signaling pathway that largely depends on the extracellular region of EphA2 and the activation of outside-in integrin signaling
The present study does not support a major role of EphA2 in cataractogenesis in an Estonian population.
Overexpression of Ephrin A2 (show EFNA2 ELISA Kits) receptor in cancer stromal cells is a prognostic factor for the relapse of gastric cancer.
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 ELISA Kits) and ephrin-A5 (show EFNA5 ELISA Kits) 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 ELISA Kits)(-/-) 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.
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.
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.
EPH receptor A2
, protein tyrosine kinase EphA2
, ephrin receptor EphA2
, ephrin type-A receptor 2
, epoxide hydrolase
, epithelial cell receptor protein tyrosine kinase
, soluble EPHA2 variant 1
, tyrosine-protein kinase receptor ECK
, epithelial cell kinase
, tyrosine-protein kinase receptor MPK-5
, tyrosine-protein kinase receptor SEK-2