Recombinant Human Ephrin-B3 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Ephrin-B3 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse 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.
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 #
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

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
Publications
Read Publication using
7924-EB in the following applications:

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.

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Publications for Ephrin-B3 (7924-EB)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol EFNB3
Uniprot