Recombinant Human Ephrin-B3 Fc Chimera Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Ephrin-B3 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human EphB3 Fc Chimera (Catalog # 432-B3) is coated at 2 μg/mL, Recombinant Human Ephrin-B3 Fc Chimera binds with an apparent K_d < 0.4 nM.
• Source: Mouse myeloma cell line, NS0-derived human Ephrin-B3 protein
  

  Human Ephrin-B3 (Leu28-Ser224) Accession # NP_001397	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: NP_001397
• N-terminal Sequence: Leu28
• Structure / Form: Disulfide-linker homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: EFNB3
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 48.3 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 57-61 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 400 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Ephrin-B3 Fc Chimera Protein, CF

• 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

Background

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 human Ephrin‑B3 consists of a 199 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 93 aa cytoplasmic domain (3, 4). Within the ECD, human Ephrin‑B3 shares 96% and 97% aa sequence identity with mouse 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).

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. Gale, N.W. et al. (1996) Oncogene 13:1343.
4. Nicola, N.A. et al. (1996) Growth Factors 13:141.
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.

Publications for Ephrin-B3 (7924-EB)(2)

Publications using 7924-EB

• ED Laing, CK Navaratnar, S Cheliout D, SR Petzing, Y Xu, SL Sterling, GA Marsh, LF Wang, M Amaya, DB Nikolov, R Cattaneo, CC Broder, K Xu Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus Proc. Natl. Acad. Sci. U.S.A., 2019-09-23;0(0):. 2019-09-23 [PMID: 31548390] (Coprecipitation Assay, Virus - Henipavirus)
• Schaupp A, Sabet O, Dudanova I, Ponserre M, Bastiaens P, Klein R The composition of EphB2 clusters determines the strength in the cellular repulsion response. J Cell Biol, 2014-01-27;204(3):409-22. 2014-01-27 [PMID: 24469634] (Bioassay, Human)

Bioinformatics

• Gene Symbol: EFNB3
• Uniprot:
  • NP_001397()