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these findings suggest that miR (zeige MLXIP Proteine)-448 functioned as a tumor suppressor gene in the development of osteosarcoma through targeting EPHA7.
the interactions of EphA5/ephrinA5 and/or EphA7/ephrinA5 between HSPCs and BMSCs, independently and cooperatively, play a role in HSPC colony formation through the upregulation of GM-CSFR. Furthermore, the adhesion/migration of HSPCs appears to be mediated in part through the activation of Rac1.
We have demonstrated the physical association and cellular co-localization of EPHA7 and EPHA10 (zeige EPHA10 Proteine) in breast carcinoma cells. The nuclear co-localization of these two receptors in invasive MDA-MB-231 cells suggests their involvement in transcriptional activation of genes involved in invasiveness.
Eph receptor A7 may have an important role in the pathogenesis of nonsmall cell lung cancer by regulating PTEN expression via thephosphatase and tensin homolog/AKT (zeige AKT1 Proteine) pathway.
Depletion of EphA7 remarkably inhibited the proliferation and invasion of Hep (zeige EPHB6 Proteine)-2 and AMC-HN-8 cells in comparison to control and EphA7 siRNA negative control (NC)-transfected cells.
Authors observed that the extracellular region of the EphA7 receptor was critical for interacting with caspase-8 (zeige CASP8 Proteine), whereas the cytoplasmic region of EphA7 was not.
miR (zeige MLXIP Proteine)-137 is able to directly bind to the EPHA7 3'UTR and negatively regulate the expression of EPHA7 in HUVECs.
MTDH (zeige MTDH Proteine) and EphA7 are markers for metastasis and poor prognosis of gallbladder adenocarcinoma.
The expression of EphA7 and/or MTDH (zeige MTDH Proteine) might be closely related to the carcinogenesis, progression, clinical biological behaviors and prognosis of gallbladder adenocarcinoma.
Overexpression of EphA7 and/or MTDH (zeige MTDH Proteine) might indicate poor prognosis in squamous cell cancer of the tongue.
The present study demonstrates that EphA7 receptors, despite their similar structure, have distinct in vivo effects on corticothalamic system projections into the ventrobasal complex /medial division of the posterior nuclear group.
Results suggest that EphA7 plays an important role in the developmental formation of cochlear innervation pattern through controlling spiral ganglion neuron fiber ontogeny
Truncated EPHA7 promotes cell reprogramming by inducing ERK (zeige EPHB2 Proteine) activity reduction.
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.
Results support the hypothesis that the anatomical organization of striatal and thalamic neurons expressing EphA7 receptors restricts the topographic distribution of cortical afferents from medial regions of S1 which express high levels of ephrin-A5 (zeige EFNA5 Proteine)
EphA4 (zeige EPHA4 Proteine)/EphA7 from the pericloacal mesenchyme signal via ephrin B2 (zeige EFNB2 Proteine) to mediate nephric duct insertion.
The role of cell-based signaling via the receptor tyrosine kinase (zeige ERBB3 Proteine) EphA7 in guiding the extension and maturation of cortical dendrites, was examined.
multi-protein complex comprising ephrinA5, EphA7, and TNFR1 (zeige TNFRSF1A Proteine) may constitute a platform for inducing caspase (zeige CASP3 Proteine)-dependent apoptotic
Data show that Dlx5 (zeige DLX5 Proteine) and Msx2 play a critical role in controlling cranial neural tube morphogenesis by regulating cell adhesion via the ephrinA5 and EphA7 pathway.
This study demonstrated a potential role for EphA/ephrin-A signaling in the initial guidance of corticofugal axons.
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.
ephrin type-A receptor 7
, EPH receptor A7
, ephrin receptor EphA7
, ephrin type-A receptor 7-like
, EPH homology kinase 3
, EPH-like kinase 11
, Eph homology kinase-3
, receptor protein-tyrosine kinase HEK11
, tyrosine-protein kinase receptor EHK-3
, developmental kinase 1
, embryonic brain kinase
, Eph-like receptor tyrosine kinase
, tyrosine-protein kinase receptor CEPHA7