• 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 binding ability in a functional ELISA. When Recombinant Mouse EphB3 Fc Chimera (Catalog # ) is coated at 2 μg/mL, Recombinant Human Ephrin-B1 Fc Chimera binds with an apparent K    _D <0.2 nM.   

• Source

  Mouse myeloma cell line, NS0-derived

  Human Ephrin-B1 (Leu28-Ser236) Accession # P98172	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Leu28

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  49.5 kDa (monomer)

• SDS-PAGE

  62-67 kDa, reducing conditions

Background: Ephrin-B1

Ephrin-B1, also known as Elk Ligand, LERK2, and Eplg2, is an approximately 45 kDa member of the Ephrin-B family of transmembrane ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. The extracellular domains (ECD) of Ephrin-B ligands are structurally related to GPI-anchored Ephrin-A ligands. Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. Ephrin-B1 preferentially interacts with receptors in the EphB family. The binding of Ephrin-B1 to EphB proteins also triggers reverse signaling through Ephrin-B1 (1, 2). Mature human Ephrin-B1 consists of a 210 amino acid (aa) ECD, a 21 aa transmembrane segment, and an 88 aa cytoplasmic domain (3, 4). Within the ECD, human Ephrin-B1 shares approximately 94% aa sequence identity with mouse and rat Ephrin-B1. Ligation by EphB2 enhances shedding of a 35 kDa fragment of the Ephrin-B1 ECD (5). The residual membrane-bound portion is then cleaved by gamma-secretase to release the intracellular domain (6). Ephrin-B1 also associates   in cis with Claudin-1, -4, and -5 (7, 8). It is expressed on glomerular podocyte slit diaphragms, developing thymocytes, peripheral T cells, monocytes, macrophages, vascular endothelial cells, cardiomyocytes, osteoclasts, and luteinizing granulosa cells in the ovary (8-13). In the developing nervous system, Ephrin-B1 plays a role in cellular migration, axon guidance, and presynaptic development (14-16). It also regulates developing thymocyte survival, monocyte migration, osteoclast differentiation and function, cardiac muscle morphogenesis, and tumorigenesis (5, 8, 10-12). Ephrin-B1 is up‑regulated on reactive astrocytes and on macrophages and T cells found in atherosclerotic plaques (11, 17).

• 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. Davis, S. et al. (1994) Science 266:816.

4. Beckmann, M.P. et al. (1994) EMBO J. 13:3757.

5. Tanaka, M. et al. (2007) J. Cell Sci. 120:2179.

6. Tomita, T. et al. (2006) Mol. Neurodegen. 1:2.

7. Tanaka, M. et al. (2005) EMBO J. 24:3700.

8. Genet, G. et al. (2012) Circ. Res. 110:688.

9. Hashimoto, T. et al. (2007) Kidney Int. 72:954.

10. Yu, G. et al. (2006) J. Biol. Chem. 281:10222.

11. Sakamoto, A. et al. (2008) Clin. Sci. 114:643.

12. Cheng, S. et al. (2012) PLoS ONE 7:e32887.

13. Egawa, M. et al. (2003) J. Clin. Endocrinol. Metab. 88:4384.

14. Davy, A. et al. (2004) Genes Dev. 18:572.

15. Bush, J.O. and P. Soriano (2009) Genes Dev. 23:1586.

16. McClelland, A.C. et al. (2009) Proc. Natl. Acad. Sci. USA 106:20487.

17. Wang, Y. et al. (2005) Eur. J. Neurosci. 21:2336.

• Entrez Gene IDs:

  1947 (Human); 13641 (Mouse); 25186 (Rat)

• Alternate Names:

  Cek5-L; EFL-3; EFNB1; ELK-L; EphrinB1; Ephrin-B1; LERK-2; STRA-1