• 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 Ephrin-B3 Fc Chimera is coated at 2 μg/mL, Recombinant Mouse EphB3 Fc Chimera (Catalog # ) binds with an apparent K    _D <1 nM.  

• Source

  Mouse myeloma cell line, NS0-derived

  Mouse Ephrin-B3 (Leu28-Ala227) Accession # O35393	IEGRMDP	Mouse IgG2A (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Leu28

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  49.2 kDa (monomer)

• SDS-PAGE

  58-61 kDa, reducing conditions

Background: Ephrin-B3

Ephrin-B3, also known as Elk-L3, LERK8, Eplg8, NLERK-2, and EFL6, is an approximately 50 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-B3 preferentially interacts with receptors in the EphB family and also with EphA4. The binding of Ephrin-B3 to Eph proteins also triggers reverse signaling through Ephrin-B3 (1, 2). Mature mouse Ephrin-B3 consists of a 200 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 92 aa cytoplasmic domain (3, 4). Within the ECD, mouse Ephrin-B3 shares 96% and 98% aa sequence identity with human and rat Ephrin-B3, respectively. Ephrin-B3 is expressed on oligodendrocytes and neurons in the hippocampus and along the midline of the spinal cord (5-9). It is up-regulated in glioma and promotes tumor cell invasion and migration (10). Ephrin-B3 functions as a repulsive axon guidance molecule by inducing growth cone collapse, neurite retraction, and axon pruning (5-8). Its repulsive effect along the spinal cord midline restricts motor neuron axons to their ipsilateral sides, thereby maintaining the independence of voluntary left side/right side movements (8, 9). Ephrin-B3 plays a role in the regulation of excitatory synapse density and synaptic maturation (6, 11, 12). It also functions as a cellular receptor for Nipah virus (13) and can induce the migration of memory B cells (14).

• 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. Tang, X.X. et al. (1997) Genomics 41:17.

4. Bergemann, A.D. et al. (1998) Oncogene 16:471.

5. Benson, M.D. et al. (2005) Proc. Natl. Acad. Sci. USA 102:10694.

6. Xu, N.-J. et al. (2011) Nat. Neurosci. 14:1421.

7. Xu, N.-J. and M. Henkemeyer (2009) Nat. Neurosci. 12:268.

8. Kullander, K. et al. (2001) Genes Dev. 15:877.

9. Yokoyama, N. et al. (2001) Neuron 29:85.

10. Nakada, M. et al. (2006) Cancer Res. 66:8492.

11. McClelland, A.C. et al. (2010) Proc. Natl. Acad. Sci. USA 107:8830.

12. Antion, M.D. et al. (2010) Mol. Cell. Neurosci. 45:378.

13. Negrete, O.A. et al. (2006) PLoS Pathog. 2:e7.

14. Holen, H.L. et al. (2011) Scand. J. Immunol. 74:144.

• Entrez Gene IDs:

  1949 (Human); 13643 (Mouse)

• Alternate Names:

  EFL-6; Efnb3; Elk-L3; EPH-related receptor tyrosine kinase ligand 8; Ephrin B3; EphrinB3; Ephrin-B3; Epl8; EPLG8EPH-related receptor transmembrane ligand ELK-L3; LERK-8; LERK8EFL6; NLERK-2