The EFNA1 Polyclonal Antibody (PAC02697) is a valuable tool for researchers studying Ephrin-A1, a critical cell surface molecule involved in various cellular processes, including cell adhesion and repulsion. This antibody, produced in rabbits, demonstrates high reactivity with human samples and is validated for Western blot applications.Ephrin-A1, a member of the Ephrin family of proteins, is known to play important roles in the development of the nervous system, angiogenesis, and tumor progression. By detecting and binding to Ephrin-A1, this antibody enables the precise detection and analysis of this protein in a wide range of cell types.
This makes it an ideal choice for studies in neuroscience, developmental biology, and cancer research.The expression and function of Ephrin-A1 have been implicated in various physiological and pathological conditions, making it a promising target for therapeutic interventions. Understanding the complex mechanisms involving Ephrin-A1 is crucial for developing targeted treatments for neurological disorders, cardiovascular diseases, and cancer. By utilizing the EFNA1 Polyclonal Antibody, researchers can uncover new insights into the role of Ephrin-A1 in health and disease, ultimately leading to the development of novel therapies.
Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis By similarity.
Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Plays an important role in angiogenesis and tumor neovascularization. The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. Exerts anti-oncogenic effects in tumor cells through activation and down-regulation of EPHA2. Activates EPHA2 by inducing tyrosine phosphorylation which leads to its internalization and degradation. Acts as a negative regulator in the tumorigenesis of gliomas by down-regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal growth cone and regulates dendritic spine morphogenesis ().
UniProt Protein Details:
NCBI Summary:
ligand of receptor tyrosine kinases; involved in thymic function and development [RGD, Feb 2006]