Recombinant Mouse Ephrin-B2 Fc Chimera Biotinylated Protein

• Reactivity: Mu
• Applications: Binding Activity

Recombinant Mouse Ephrin-B2 Fc Chimera Biotinylated Protein Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized recombinant mouse EphB2 Fc Chimera at 2 µg/mL (100 µL/well) can bind Biotinylated Recombinant Mouse Ephrin-B2 Fc Chimera with a linear range of 0.039-2.5 ng/mL.
  Optimal dilutions should be determined by each laboratory for each application.
• Source: Mouse myeloma cell line, NS0-derived mouse Ephrin-B2 protein
  

  Mouse Ephrin-B2 (Arg27 - Ala227) Accession # AAA82934	DIEGRMD	Human IgG1 (Pro100 - Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: AAA82934
• N-terminal Sequence: Arg27
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Efnb2
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 49.6 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: 60-65 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: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse Ephrin-B2 Fc Chimera Biotinylated Protein

• EFNB2
• ELF-2
• ephrin B2
• EphrinB2
• Ephrin-B2
• EPLG5
• HTKL
• Htk-L
• LERK5
• LERK-5
• NLERK-1

Background

Ephrin‑B2, also known as Htk‑L, ELF‑2, LERK‑5, and NLERK‑1, is a 40 kDa member of the Ephrin‑B family of transmembrane ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. The extracellular domains 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‑B2 preferentially interacts with receptors in the EphB family (1, 2). Mature mouse Ephrin‑B2 consists of a 204 amino acid (aa) extracelluar domain (ECD), a 21 aa transmembrane segment, and an 83 aa cytoplasmic domain [Cerretti 1197, Bergemann 4921, Bennett 1866]. Within the ECD, mouse Ephrin‑B2 shares 97% and 98% aa sequence identity with human and rat Ephrin‑B2, respectively. Ephrin‑B2 is expressed presynaptically on neurons (6, 7). It promotes presynaptic development, EphB2 shedding, axonal growth cone collapse, and neurite repulsion, and also regulates inflammatory and neuropathic pain (6 ‑ 8). Ephrin‑B2 is expressed by vascular mural cells and arterial vascular and lymphatic endothelium (9, 10). It exerts proliferative and migratory effects on these cells during angiogenesis and lymphangiogenesis in part by regulating the signaling activity of VEGF R2 and VEGF R3 (8 ‑ 11). Ephrin‑B2 plays a role in the immune response by mediating monocyte extravasation and T cell costimulation (12, 13). It is upregulated in invasive cancers and promotes tumor cell migration, invasion, and tumor angiogenesis (14  ‑ 16). It functions as a cellular entry receptor for Hendra and Nipah viruses (17). Ephrin‑B2 is also important for the separation of the urinary and intestinal tracts during development (18).

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. Cerretti, D.P. et al. (1995) Mol. Immunol. 32:1197.
4. Bergemann, A.D. et al. (1995) Mol. Cell. Biol. 15:4921.
5. Bennett, B.D. et al. (1995) Proc. Natl. Acad. Sci. 92:1866.
6. McClelland, A.C. et al. (2009) Proc. Natl. Acad. Sci. 106:20487.
7. Zhao, J. et al. (2010) Mol. Pain 6:77.
8. Lin, K.-T. et al. (2008) J. Biol. Chem. 283:28969.
9. Foo, S.S. et al. (2006) Cell 124:161.
10. Wang, Y. et al. (2010) Nature 465:483.
11. Sawamiphak, S. et al. (2010) Nature 465:487.
12. Pfaff, D. et al. (2008) J. Cell Sci. 121:3842.
13. Yu, G. et al. (2003) J. Immunol. 171:106.
14. Meyer, S. et al. (2005) Int. J. Oncol. 27:1197.
15. Nakada, M. et al. (2010) Int. J. Cancer 126:1155.
16. Liu, W. et al. (2004) Br. J. Cancer 90:1620.
17. Bonaparte, M.I. et al. (2005) Proc. Natl. Acad. Sci. 102:10652.
18. Dravis, C. et al. (2004) Dev. Biol. 271:272.

Publications for Ephrin-B2 (BT496)(3)

Publications using BT496

• 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, Mouse)
• A Di Rubbo, L McNabb, R Klein, JR White, A Colling, DS Dimitrov, CC Broder, D Middleton, RA Lunt Optimization and Diagnostic Evaluation of Monoclonal Antibody-based Blocking ELISA Formats for Detection of Neutralizing Antibodies to Hendra Virus in Mammalian Sera J. Virol. Methods, 2019-09-09;274(0):113731. 2019-09-09 [PMID: 31513861] (Bioassay, ELISA Detection, Virus - Hendra)
• Moza B, Varma AK, Buonpane RA, Zhu P, Herfst CA, Nicholson MJ, Wilbuer AK, Seth NP, Wucherpfennig KW, McCormick JK, Kranz DM, Sundberg EJ Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1. EMBO J., 2007-02-01;26(4):1187-97. 2007-02-01 [PMID: 17268555] (Surface Plasmon Resonance, Mouse)

Bioinformatics

• Gene Symbol: Efnb2
• Uniprot:
  • AAA82934()