Recombinant Human Ephrin-B3 Fc Chimera Biotinylated Protein

• Reactivity: Hu
• Applications: Binding Activity

Recombinant Human Ephrin-B3 Fc Chimera Biotinylated Protein Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized recombinant mouse EphB3 Fc Chimera at 2 µg/mL (100 µL/well) can bind biotinylated Recombinant Human Ephrin‑B3 Fc Chimera with a linear range of 1.3-80 ng/mL.
  Optimal dilutions should be determined by each laboratory for each application.
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Ephrin-B3 protein
  

  Human Ephrin-B3 (Leu28-Ser224) Accession # Q15768	IEGRMD	Human IgG1 (Pro100-Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: Q15768
• N-terminal Sequence: Leu28
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: EFNB3
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 49.2 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: 58 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 with BSA as a carrier protein.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions:

  Reconstitute at 100 μg/mL with sterile 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 Biotinylated Protein

• 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 (BT395)(3)

Publications using BT395

• Y Li, R Li, M Wang, Y Liu, Y Yin, X Zai, X Song, Y Chen, J Xu, W Chen Fc-Based Recombinant Henipavirus Vaccines Elicit Broad Neutralizing Antibody Responses in Mice Viruses, 2020-04-23;12(4):. 2020-04-23 [PMID: 32340278] (Bioassay, Human)
• SH Park, MJ Jo, BR Kim, YA Jeong, YJ Na, JL Kim, S Jeong, HK Yun, DY Kim, BG Kim, SH Kang, SC Oh, DH Lee Sonic hedgehog pathway activation is associated with cetuximab resistance and EPHB3 receptor induction in colorectal cancer Theranostics, 2019-04-12;9(8):2235-2251. 2019-04-12 [PMID: 31149041] (Bioassay, Human)
• Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, Human)

Bioinformatics

• Gene Symbol: EFNB3
• Uniprot:
  • Q15768()