Mouse myeloma cell line NS0-derived recombinant human EphA1 Arg24-Glu547 (predicted) Accession # P21709
Detects human EphA1 in direct ELISAs and Western blots. No cross-reactivity with recombinant mouse EphA2, A3, A4, A6, A7, A8, B2, B4, B5, B6, recombinant rat (rr) EphA5, rrEphB1, or recombinant human EphB1 is observed.
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EphA1, also known as Eph and Esk (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. This is followed by the transmembrane region and cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxy tail which contains one conserved tyrosine residue. Activation of kinase activity occurs after ligand recognition and binding. EphA1 has been shown to bind ephrin-A1 (2, 3). The extracellular domains of mouse and human EphA1 share greater than 91% 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).
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