Human Ephrin-A4 Biotinylated Antibody
Human Ephrin-A4 Biotinylated Antibody Summary
Accession # P52798
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Ephrin-A4, also known as LERK-4 and EFL-4, (1) is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor binding domain. This conserved sequence consists of approximately 125 amino acids and includes four invariant cysteines. The A-class ligands have a GPI anchor following the conserved sequence. Ephrin-A4 has been shown to bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1 (2, 3). The extracellular domains of human and mouse Ephrin-A4 share 80% amino acid identity. Only membrane-bound or Fc-clustered ligands are capable of activating the receptor in vitro. While soluble monomeric ligands bind the receptor, they do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all receptors and ligands are expressed in developing and adult neural tissue (3). The Eph/ephrin families also appear to play a role in angiogenesis (3).
- Eph Nomenclature Committee [letter] (1997) Cell 90:403.
- Flanagan, J.G. and P. Vanderhaegen (1998) Annu. Rev. Neurosci. 21:309.
- Pasquale, E.B. (1997) Curr. Opin. Cell. Biol. 9:608.
Citation for Human Ephrin-A4 Biotinylated Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
A new ephrin-A1 isoform (ephrin-A1b) with altered receptor binding properties abrogates the cleavage of ephrin-A1a.
Authors: Finne EF, Munthe E, Aasheim HC
Biochem. J., 2004;379(0):39-46.
Sample Types: Whole Cells
Applications: Flow Cytometry
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