EphA2 Antibody (1C1) - Azide and BSA Free

Recombinant Monoclonal Antibody

1C1 was isolated after screening of a non-immunized human Fab phage library. Selection was based on the ability to bind soluble human recombinant EphA2 (residues 183-510). The Fab was subsequently converted to full length human IgG1.

1C1 binds specifically to the amino-termianal LBD (ligand-binding domain) region of the EphA2 ectodomain (IgG1 KD ~0.8 nM; Fab KD ~140 nM) and not to other related human Eph receptors such as EphA1, EphA2, and EphA4, or any EphB receptor family members.

IgG1 Kappa

Monoclonal

Human

EPHA2

Protein A purified

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This antibody binds to human Ephrin type-A receptor 2, a receptor tyrosine kinase that binds to membrane-bound ephrin-A ligands residing on adjacent cells, triggering contact-dependent signaling into neighboring cells. Eph2A is involved in pattern formation during development, angiogenesis and osteoblastogenesis. Eph2A has also been found to be expressed in a variety of cancers. This antibody acts as an agonist of Eph2A signaling. The agonist properties of 1C1 is due to ligand mimicry by VDR3. After cell binding, the antibody is able to induce rapid tyrosine phosphorylation, internalization, and degradation of the EphA2 receptor.