• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to inhibit proliferation of PC‑3 human prostate cancer cells. The ED    ₅₀ for this effect is 5-25 ng/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Human Ephrin-A2 (Glu27-Asn188) Accession # O43921	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Starts at Glu27

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  45.1 kDa (monomer)

• SDS-PAGE

  55-60 kDa, reducing conditions

Background: Ephrin-A2

Ephrin‑A2, also known as ELF‑1, HEK7‑L, LERK‑6, and EPLG6, is an approximately 20 kDa member of the GPI‑linked Ephrin‑A family of proteins that bind and induce the tyrosine autophosphorylation of Eph receptors. In particular, Ephrin‑A2 preferentially interacts with receptors of the EphA family of proteins. Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, axon guidance and cancer progression. (1‑3). Human Ephrin‑A2 is synthesized as a 213 amino acid (aa) preproprecursor that contains a 24 aa signal peptide, a 164 aa mature chain, and a 25 aa C‑terminal propeptide that is removed prior to GPI linkage of Ephrin‑A2 to the membrane (4, 5). The mature region is structurally related to the extracellular domains of the transmembrane Ephrin‑B ligands (1, 3), and shares 93% aa sequence identity with mouse and rat Ephrin‑A2. Ephrin‑A2 is expressed in discrete regions of the developing nervous system and limb buds (6‑9). Its distribution complements the pattern of Eph receptor expression, and this plays an important role in tissue morphogenesis (9‑11). Ephrin‑A2 exerts an axon repulsive signal which is important for the accurate pathfinding of retinal ganglion cell axons to the tectum and hippocampal axons to the lateral septum (10, 12). Its up‑regulation on astrocytes at sites of optic nerve damage may prevent re‑innervation by retinal ganglion cells (13). Ephrin‑A2 is also expressed on neural progenitor cells in the subventricular zone (SVZ). It interacts with EphA7, triggering reverse signaling through Ephrin‑A2 and inhibition of progenitor cell proliferation (10). In the developing limbs, Ephrin‑A2 regulates cartilage morphogenesis and the projection of motoneuron axons (8, 9, 14).

• References:

1. Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.

2. Astin, J.W. et al. (2010) Nat. Cell Biol. 12:1194.

3. Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.

4. Aasheim, H.-C. et al. (1998) Biochem. Biophys. Res. Commun. 252:378.

5. Cerretti, D.P. and N. Nelson (1998) Genomics 47:131.

6. Cheng, H.-J. et al. (1994) Cell 79:157.

7. Kenmuir, C.L. et al. (2012) Anat. Rec. (Hoboken) 295:105.

8. Ohta, K. et al. (1997) Mech. Dev. 64:127.

9. Wada, N. et al. (2003) Dev. Biol. 264:550.

10. Gao, P.-P. et al. (1996) Proc. Natl. Acad. Sci. USA 93:11161.

11. Holmberg, J. et al. (2005) Genes Dev. 19:462.

12. Nakamoto, M. et al. (1996) Cell 86:755.

13. Symonds, A.C.E. et al. (2007) Eur. J. Neurosci. 25:744.

14. Eberhart, J. et al. (2000) Dev. Neurosci. 22:237.

• Entrez Gene IDs:

  1943 (Human); 13637 (Mouse)

• Alternate Names:

  Cek7-L; EFNA2; ELF-1; EPH-related receptor tyrosine kinase ligand 6; EphrinA2; Ephrin-A2; EPLG6HEK7 ligand; HEK7-L; HEK7-ligand; LERK6; LERK6LERK-6; ligand of eph-related kinase 6