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anti-Mouse (Murine) Ephrin A1 Antibodies:
anti-Rat (Rattus) Ephrin A1 Antibodies:
anti-Human Ephrin A1 Antibodies:
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Mouse (Murine) Polyclonal Ephrin A1 Primary Antibody for ELISA, WB - ABIN4308733
Zhang, Zeng, Briggs, Beaty, Simons, Chiu Yen, Tyler, Tsai, Ye, Gesell, Herman, Baylin, Watkins: A potential tumor suppressor role for Hic1 in breast cancer through transcriptional repression of ephrin-A1. in Oncogene 2010
In myelinating co-cultures and in zebrafish, we find that the number of mature oligodendrocytes does not change as result of manipulating signaling through the ephrinA1-EphA4 system. However, in both systems, inhibition of EphA4 signaling leads to a higher number of myelin sheaths formed by each oligodendrocyte. In isolated oligodendrocyte cultures, activation of EphA4 reduced process extension.
By using MALDI-MSI, this study simultaneously shows the distribution and spatial localization of ephrin A1, as well as additional cardiac proteins, thus offering valuable information for the elucidation of molecular partners, mediators, and targets of ephrin A1 action in cardiac muscle.
EphA2 mAb treatment could partially inhibit LPSinduced inactivation of EphBEphrin B3 signalling, while Ephrin B3 overexpression could abrogate LPSinduced activation of EphA2Ephrin A1 signalling. EphB1/Ephrin B3 signalling may antagonise the EphA2/Ephrin A1dependent pathway following LPS treatment.
Collectively, these data suggest that ATRA attenuates bleomycin-induced pulmonary fibrosis by regulating EphA2-EphrinA1 and PI3K-Akt signaling.
Lipopolysaccharide exposure significantly up-regulated EphA2 and EphrinA1 expression.
Activation of EphA1-Epha receptor axis attenuates diabetic nephropathy in mice.
Following ephrin-A1 stimulation, truncated EphA2 did not detectably interfere with the phosphorylation of endogenous EphA2, and it potentiated cell adhesion possibly through modulation of integrin avidity.
ADAM12 enhanced ephrin-A1 cleavage in response to transforming growth factor-betra1 in primary tumors.
S100A8 and ephrin-A1 contribute to lung metastasis.
We used in utero electroporation-mediated EphA7 overexpression in developing somatosensory corticothalamic axons to dissect EphA7/ephrin-A-dependent mechanisms involved in regulating both initial targeting and postnatal growth of the CT projections.
Elevated levels of ephrin-A1 may contribute to diabetic keratopathies by persistently engaging EphA2 and prohibiting Akt-dependent corneal epithelial repair processes.
Data indicate that ephrin-A1 regulates cardiac valve development, making ephrin-A1-deficient mice a novel model for congenital heart defects.
Cooperation between Slit2 and ephrin-A1 regulates a balance between the pro- and antiangiogenic functions of Slit2.
ephrin-A1 has a positive role in tumor growth in vivo, and are consistent with previous reports of ephrin-A1 acting through EphA receptors in the tumor microenvironment in vivo.
When NIH3T3 cells were plated onto an ephrinA1-coated surface, the cells both adhered and spread.
Immunohistological analyses reveal strong ephrin-A1 expression in lung tissue, low expression in cortical areas of lymph nodes, and none in T cell/B cell areas of the spleen.
Whole-mount in situ hybridization revealed overlapping expression of the Epha1 receptor and its high-affinity ligands ephrin A1 (Efna1) and ephrin A3 (Efna3) in the primitive streak and the posterior paraxial mesoderm during early mouse development.
Ephrins A1 and A5 are substrates for a cross-linking enzyme, tissue transglutaminase, which mediates the formation of oligomeric ephrin.
Increased expression of ephrin-A1 accelerated the malignant progression of the intestinal adenoma to invasive tumors.
HIF-2alpha plays an essential role in vascular remodeling during tumor vascularization through activation of at least ephrin A1.
Radiotherapy-induced changes in ephrin-A1 gene expression related with angiogenesis may modulate microenvironment and influence responsiveness of tumors.
The lncRNA referred to as GMAN is part of the EFNA1 locus.
A case-control study revealed no significant association between the rs12904 polymorphism in the 3'-untranslated region of ephrin A1 ligand and the risk of sporadic colorectal cancer in Iranian population.
We created a novel pH-dependent transmembrane peptide, TYPE7, by altering the sequence of the transmembrane domain of EphA2..TYPE7 binds to endogenous EphA2 and reduces Akt phosphorylation and cell migration as effectively as ephrinA1
ephrin-A1 seems to be remarkably involved in elementary processes of endothelial migration like cellular polarization, migratory direction and speed.
Findings show that EFNA1 expression is a useful marker for predicting a high risk of recurrence in hepatocellular carcinoma patients but not EPHA2.
Results suggest that EFNA1 is involved in colorectal tumorigenesis, and rs12904 A>G polymorphism in the 3' UTR of EFNA1 is associated with CRC susceptibility in a Chinese population.
EphA2-ephrinA1 trans-endocytosis is sensitive to the mechanical properties of a cell's microenvironment
Ephrin-A1 is upregulated in tumor microenvironment and promotes angiogenesis through a coordinated cross-talk with PI3K/Akt-dependent eNOS activation.
The interaction between ephrin-As, Eph receptors and integrin alpha3 is plausibly important for the crosstalk between Eph and integrin signalling pathways at the membrane protrusions and in the migration of brain cancer cells.
Increased expression of EFNA1 mRNA is associated with gastric cancer.
Expression of EPHRIN-A1 tends to be associated with worse survival in head and neck cancer.
EFNA1 expression is a useful marker for predicting high risk of relapse and cancer-related death in patients who have undergone curative resection for CRC.
Findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
present study showed a high expression of EphA2/ephrinA1 in adenoid cystic carcinoma. EphA2/ephrinA1 can serve as a novel therapy target for adenoid cystic carcinoma.
EphA2 activation by ephrin-A1 induces tumor suppressor gene cdx-2 expression which attenuates cell proliferation, tumor growth and thus may be a promising therapeutic target against NSCLC.
in p-stage I NSCLC patients, those in the higher EphA2 expression and higher ephrin-A1 expression groups shared almost the same clinicopathological backgrounds which are generally considered to be better prognostic factors.
The EphA2 ligand EphrinA1 induces EphA2 phosphorylation and intracellular internalization and degradation, thus inhibiting breast tumor progression.
Multiple oncogenic signalling pathways are affected by ephrin-A1, from the promotion of a specific pathway in one cell or cancer type to the inhibition of the same pathway in another type of cell or cancer. [Review]
Ovarian serous carcinomas and ovarian cancer cell lines overexpress EphA2 and EphrinA-1. Tumor patients with higher expression levels of both EphA2 and EphrinA-1 have a significantly poorer clinical outcome.
The Eph-ephrinA system can promote cell attachment along with intercellular dissociation.
expression of Eph A1, A2, A4, and A7 was strongly detected in endometrial epithelial cells during early pregnancy.
The Eph-Ephrin A system might play an important role in regulating the swine contact between blastocysts and endometrium during embryo implantation.
Eph A-ephrin A1 system is a positive factor in the increase and maintenance of epithelial cells in mammary glands of cows; the signaling system contributes to development, remodeling, and functionality of normal mammary glands and could overcome mastitis.
This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. 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. This gene encodes an EFNA class ephrin which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis.
EPH-related receptor tyrosine kinase ligand 1
, eph ligand family-a
, ephrin A1
, immediate early response protein B61
, TNF alpha-induced protein 4
, eph-related receptor tyrosine kinase ligand 1
, ligand of eph-related kinase 1
, tumor necrosis factor alpha-induced protein 4
, tumor necrosis factor, alpha-induced protein 4
, ephrin-A1 b