• Purity

  >90%, 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 binding ability in a functional ELISA. Immobilized rmEphA2/Fc Chimera at 2 µg/mL (100 µL/well) can bind rmEphrin-A1 Fc Chimera with a linear range of 0.16-10 ng/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Mouse Ephrin-A1 (Asp19 - Ser182) Accession # P52793	IEGRMD	Human IgG1 (Pro100 - Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Asp19

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  46.8 kDa (monomer)

• SDS-PAGE

  50-55 kDa, reducing conditions

Background: Ephrin-A1

Ephrin-A1, also known as B61 and LERK-1, is a member of the Ephrin-A family of GPI-anchored ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. Ephrin-A ligands are structurally related to the extracellular domains of the transmembrane Ephrin-B ligands. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1, 2). Mouse Ephrin-A1 is synthesized with an 17 amino acid (aa) signal peptide, a 165 aa mature chain, and a 23 aa C‑terminal propeptide which is removed prior to GPI linkage of Ephrin-A1 to the membrane (3, 4). It can also be released as a soluble molecule (3, 5, 6). The mature 21 ‑ 25 kDa mouse Ephrin-A1 shares 85% and 94% aa sequence identity with human and rat Ephrin-A1, respectively. Ephrin-A1 is widely expressed on endothelial and epithelial cells, particularly in the lung, intestine, liver, and skin (4, 8). It is expressed on resting CD4+ T cells but is down‑regulated following activation (7, 8). Ligation of Ephrin-A1 on CD4+ T cells inhibits cell proliferation and activation, although soluble Ephrin-A1 can promote T cell chemotaxis (7, 8). In cancer, Ephrin‑A1 is expressed by tumor cells as well as on the tumor-associated vasculature (5, 6, 9). It inhibits tumor cell proliferation and migration but also supports tumor growth by promoting angiogenesis (10 - 12). Soluble Ephrin-A1 additionally promotes neuronal survival and neurite extension (13).

• References:

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

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

3. Takahashi, H. and T. Ikeda (1995) Oncogene 11:879.

4. Shao, H. et al. (1995) J. Biol. Chem. 270:5636.

5. Easty, D.J. et al. (1995) Cancer Res. 55:2528.

6. Cui, X.-D. et al. (2010) Int. J. Cancer 126:940.

7. Wohlfahrt, J.G. et al. (2004) J. Immunol. 172:843.

8. Aasheim, H.-C. et al. (2005) Blood 105:2869.

9. Ogawa, K. et al. (2000) Oncogene 19:6043.

10. Liu, D.-P. et al. (2007) Int. J. Oncol. 30:865.

11. Brantley-Sieders, D.M. et al. (2006) Cancer Res. 66:10315.

12. Pandey, A. et al. (1995) Science 268:567.

13. Magal, E. et al. (1996) J. Neurosci. Res. 43:735.

• Entrez Gene IDs:

  1942 (Human); 13636 (Mouse)

• Alternate Names:

  B61; ECKLG; EFL1; EFL-1; EFNA1; EPH-related receptor tyrosine kinase ligand 1; EphrinA1; Ephrin-A1; EPLG1TNF alpha-induced protein 4; Immediate early response protein B61; LERK1; LERK1LERK-1; ligand of eph-related kinase 1; TNFAIP4B61; Tumor necrosis factor alpha-induced protein 4; tumor necrosis factor, alpha-induced protein 4