Phospho-EphA3/4/5 (Y779/833) Polyclonal Antibody, 100µg, (ATB-P1041)

Description

Background:

This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. Two alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Jul 2008]

Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands 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. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.

Product datasheet:

References:

1. Genome-wide copy number variation in sporadic amyotrophic lateral sclerosis in the Turkish population: deletion of EPHA3 is a possible protective factor. Uyan Ö, et al. PLoS One, 2013. PMID 23991104 Free PMC Article
2. High levels of EphA3 expression are associated with high invasive capacity and poor overall survival in hepatocellular carcinoma. Lu CY, et al. Oncol Rep, 2013 Nov. PMID 23970317
3. EphA3 maintains tumorigenicity and is a therapeutic target in glioblastoma multiforme. Day BW, et al. Cancer Cell, 2013 Feb 11. PMID 23410976
4. A high-content cellular senescence screen identifies candidate tumor suppressors, including EPHA3. Lahtela J, et al. Cell Cycle, 2013 Feb 15. PMID 23324396 Free PMC Article
5. Effects of cancer-associated EPHA3 mutations on lung cancer. Zhuang G, et al. J Natl Cancer Inst, 2012 Aug 8. PMID 22829656 Free PMC Article
6. Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines.
   Wicks I.P., Wilkinson D., Salvaris E., Boyd A.W.
   Proc. Natl. Acad. Sci. U.S.A. 89:1611-1615(1992) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-924.
7. Identification of a tumor-specific shared antigen derived from an Eph receptor and presented to CD4 T cells on HLA class II molecules.
   Chiari R., Hames G., Stroobant V., Texier C., Maillere B., Boon T., Coulie P.G.
   Cancer Res. 60:4855-4863(2000) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Melanoma.
8. Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell line.
   Boyd A.W., Ward L.D., Wicks I.P., Simpson R.J., Salvaris E., Wilks A., Welch K., Loudovaris M., Rockman S., Busmanis I.
   J. Biol. Chem. 267:3262-3267(1992) [PubMed] [Europe PMC] Cited for: PROTEIN SEQUENCE OF 21-29 AND 840-860, CHARACTERIZATION.
9. Unified nomenclature for Eph family receptors and their ligands, the ephrins.
   Eph nomenclature committee
   Cell 90:403-404(1997) [PubMed] [Europe PMC] Cited for: NOMENCLATURE.
10. Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling.
    Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
    J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] Cited for: FUNCTION IN CELL-CELL ADHESION, EFNA5-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-596; TYR-602 AND TYR-779.