Recombinant Human Ephrin-B3 Fc Chimera Protein, CF

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Recombinant Human Ephrin-B3 Fc Chimera Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
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 Kd < 0.4 nM.
Mouse myeloma cell line, NS0-derived human Ephrin-B3 protein
Human Ephrin-B3
Accession # NP_001397
N-terminus C-terminus
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linker homodimer
Predicted Molecular Mass
48.3 kDa (monomer)
57-61 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 400 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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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 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.
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

Citations for Recombinant Human Ephrin-B3 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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  1. Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus
    Authors: 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
    Proc. Natl. Acad. Sci. U.S.A., 2019-09-23;0(0):.
    Species: Virus - Henipavirus
    Sample Types: Recombinant Protein
    Applications: Coprecipitation Assay
  2. The composition of EphB2 clusters determines the strength in the cellular repulsion response.
    Authors: Schaupp A, Sabet O, Dudanova I, Ponserre M, Bastiaens P, Klein R
    J Cell Biol, 2014-01-27;204(3):409-22.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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