|Other Names||Ephrin-A4, EPH-related receptor tyrosine kinase ligand 4, LERK-4, EFNA4, EPLG4, LERK4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8835c was selected from the Center region of human EFNA4. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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. May play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.|
|Cellular Location||Isoform 1: Cell membrane; Lipid-anchor, GPI- anchor|
|Tissue Location||Expressed in the adult spleen, lymph node, prostate, ovary, small intestine, and colon, and in fetal heart, lung, liver and kidney. Also detected in hematopoietic cell lines|
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Provided below are standard protocols that you may find useful for product applications.
EFNA4 is 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.
Flanagan,J.G. et.al., Annu. Rev. Neurosci. 21, 309-345 (1998)
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