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EFNA5 / Ephrin A5 Antibody (aa31-80)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, IF, E |
|---|---|
| Primary Accession | P52803 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 26kDa |
| Dilution | ELISA (1:40000), IF (1:100-1:500), IHC-P (10 µg/ml), WB (1:500-1:1000) , |
| Gene ID | 1946 |
|---|---|
| Other Names | Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7, LERK-7, EFNA5, EPLG7, LERK7 |
| Target/Specificity | EFNA5 Antibody detects endogenous levels of total EFNA5 protein. |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. |
| Precautions | EFNA5 / Ephrin A5 Antibody (aa31-80) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | EFNA5 |
|---|---|
| Synonyms | EPLG7, LERK7 |
| Function | 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. |
| Cellular Location | Cell membrane; Lipid-anchor, GPI-anchor. Membrane, caveola; Lipid-anchor, GPI-anchor. Note=Compartmentalized in discrete caveolae-like membrane microdomains |
| Volume | 50 µl |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Winslow J.W.,et al.Neuron 14:973-981(1995).
Kozlosky C.J.,et al.Cytokine 9:540-549(1997).
Davy A.,et al.Genes Dev. 13:3125-3135(1999).
Lawrenson I.D.,et al.J. Cell Sci. 115:1059-1072(2002).
Janes P.W.,et al.Cell 123:291-304(2005).
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