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Biochem/physiol Actions

EPHA2 binds to the ephrin-A ligand and has diverse cellular function. EPHA2 has been shown to be an oncoprotein of importance in a range of cancers. EPHA2 is overexpressed in several human cancer types and promotes malignancy through a mechanism involving RhoA-dependent destabilization of adherens junctions. EPHA2 overexpression induces a FAK-dependent increase in MMP-2 expression and invasiveness and this process can be reversed by ligation of EPHA2.

General description

EPHA2 (ephrin receptor A2) belongs to the Eph family of receptor tyrosine kinases. It is a type I transmembrane protein, and its exoplasmic domain consists of a ligand binding domain in its N-terminal, a cysteine-rich domain, and two fibronectin type III repeats. Its cytoplasmic domain contains a juxtamembrane region, a tyrosine kinase domain, a SAM (sterile-α-motif) motif, and a PDZ-binding domain.

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Physical form

Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.