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During urogenital development, different modes of Eph (show EPHA1 Proteins)/Ephrin signaling occur at several sites with EphrinB2 (show EFNB2 Proteins) and EphrinA5 acting in concert.
dissociations of N-cadherin (show CDH2 Proteins) and adherens junctions in the associated interlocking domains may result in the formation of isolated globules and nuclear opacities in the ephrin-A5(-/-) mice.
Overexpression of Ephrin-A5 in mice results in decreasing the size of progenitor pool through inducing apoptosis.
Ephrin-A5 interacts with Ephrin-A4 (show EFNA4 Proteins) to modulate neurogenesis and angiogenesis in a model of temporal lobe epilepsy.
Data show the effects of genetic loss of ephrin-A5, Eph receptors EphA4, and EphA7 on the development of medulloblastoma tumors in the smoothened (Smo) transgenic mouse model.
the unique cross-subclass interaction of EphB2 (show EPHB2 Proteins) with ephrin A5 has evolved to function upstream of JNK (show MAPK8 Proteins) signaling for the purpose of maintaining an adequate pool of progenitor cells to ensure proper closure of the optic fissure.
Female mice lacking EFNA5 are subfertile, exhibit a compromised response to LH, and display abnormal ovarian histology after superovulation.
NF-kappaB (show NFKB1 Proteins) in NG2 (show Vcan Proteins)(+) cells promotes myoblast migration to the tips of myofibers through cell-cell contact through expression of ephrinA5 from NG2 (show Vcan Proteins)(+) cells
The reduced nuclear size and diminished gene expression mirrors subtle changes in ephrin A5 expression evident in P1 and P4 enucleated neocortex, 11 and 8 days prior to natural eye opening, respectively.
These data support the hypothesis that the retinocollicular projection is a superimposition of a number of individual two-dimensional topographic maps that originate from specific types of RGCs, require ephrin-A signaling.
These results indicate a novel mechanism of ephrin-Eph (show EPHA1 Proteins) signaling independent of direct cell contact and proteolytic cleavage and suggest the participation of EphB2 (show EPHB2 Proteins)(+) extracellular vesicles in neural development and synapse physiology.
MiR (show MLXIP Proteins)-96 and miR (show MLXIP Proteins)-182 are upregulated in hepatocellular carcinoma and negatively associated with ephrin A5 expression.
the structure of the ligand-binding domain of the EphA3 (show EPHA3 Proteins) receptor in complex with its preferred ligand, ephrin-A5, is reported.
Data indicate that ephrin-A5 binding directly facilitates the formation of Eph (show EPHA1 Proteins)/ephrin clusters by inducing conformational changes in the ligand-binding domain (LBD) of EphA4 (show EPHA4 Proteins).
Transgenic ephrin-A5 plays a critical role in postnatal lens fiber organization to maintain lens transparency: cells in the ephrin-A5-deficient lens are severely disorganized
This study presented that EFNA5 showed strong associations with alcohol withdrawal symptoms.
Data suggest that ephrinA5 mRNA/protein levels are reduced in colon adenocarcinoma compared to normal colon tissue; staging/grading indicates that ephrinA5 inhibits colon adenocarcinoma progression via c-Cbl (show CBL Proteins)-mediated EGFR (show EGFR Proteins) ubiquitination/degradation.
analysis of molecular surfaces in ephrin-A5 essential for a functional interaction with EphA3 (show EPHA3 Proteins)
ephrin-A5-induced cell-morphologic changes of EphA3 (show EPHA3 Proteins)-positive LK63 pre-B acute lymphoblastic leukemia cells
These observations indicate that only a subset of signal transduction pathways is required for ephrin-A5-induced growth cone collapse.
Treatment of the bovine satellite cells (BSC (show SLC12A2 Proteins)) with ephrin-A5 causes a reduction in velocity with a concomitant increase in directed migration. Treatment of BSC (show SLC12A2 Proteins) with hepatocyte growth factor (show HGF Proteins) had no immediate effect on cell motility or migration.
Ephrin-A5, a member of the ephrin gene family, prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.
, ephrin A5
, EPH-related receptor tyrosine kinase ligand 7
, eph-related receptor tyrosine kinase ligand 7
, repulsive axon guidance signal protein