EFNA5 (基因名), Ephrin-A5 (蛋白名), efna5_human.
产品名称:
Human EFNA5/ Ephrin-A5 CLIA Kit
货号:
U10772h
商标:
EIAab®
监管等级:
别名:
AL-1, EPH-related receptor tyrosine kinase ligand 7, LERK-7, EPLG7, LERK7
检测方法:
CLIA
特异性:
Natural and recombinant human Ephrin-A5
样品类型:
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
样品数据:
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研究领域:
-
通用注释
亚单元:
Binds to EPHB2. Interacts with EPHA8; activates EPHA8 (By similarity). Binds to the receptor tyrosine kinases EPHA2, EPHA3 and EPHB1. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function.
功能:
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. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.
亚细胞位置:
Cell membrane
Lipid-anchor
GPI-anchor
Membrane
Caveola
Lipid-anchor
GPI-anchor
Compartmentalized in discrete caveolae-like membrane microdomains.
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