Recombinant Mouse Ephrin-B1 Fc Chimera Biotinylated Protein

• Reactivity: Mu
• Applications: Binding Activity

Recombinant Mouse Ephrin-B1 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 Mouse Ephrin‑B1 Fc Chimera with a linear range of 0.078-1.25 ng/mL.
  Optimal dilutions should be determined by each laboratory for each application.
• Source: Mouse myeloma cell line, NS0-derived mouse Ephrin-B1 protein
  

  Human Ephrin-B1 (Lys30-Ser229) Accession # Q544L9	IEGRMD	Human IgG1 (Pro100-Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: Q544L9
• N-terminal Sequence: Lys30
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Efnb1
• 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: 60 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 with sterile PBS at 100 μg/mL.

Notes

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

Alternate Names for Recombinant Mouse Ephrin-B1 Fc Chimera Biotinylated Protein

• Cek5-L
• EFL3
• EFL-3
• EFNB1
• ELK ligand
• ELK-L
• EphrinB1
• Ephrin-B1
• LERK-2
• STRA-1

Background

Ephrin-B1, also known as Elk Ligand, LERK2, and Eplg2, is an approximately 45 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-B1 preferentially interacts with receptors in the EphB family. The binding of Ephrin-B1 to EphB proteins also triggers reverse signaling through Ephrin-B1 (1, 2). Mature mouse Ephrin-B1 consists of a 212 amino acid (aa) ECD, a 21 aa transmembrane segment, and an 88 aa cytoplasmic domain (3, 4). Within the ECD, mouse Ephrin-B1 shares 94% and 98% aa sequence identity with human and rat Ephrin-B1, respectively. Ligation by EphB2 enhances shedding of a 35 kDa fragment of the Ephrin-B1 ECD (5). The residual membrane-bound portion is then cleaved by gamma-secretase to release the intracellular domain (6). Ephrin-B1 also associates in cis with Claudin-1, -4, and -5 (7, 8). It is expressed on glomerular podocyte slit diaphragms, developing thymocytes, peripheral T cells, monocytes, macrophages, vascular endothelial cells, cardiomyocytes, osteoclasts, and luteinizing granulosa cells in the ovary (8-13). In the developing nervous system, Ephrin-B1 plays a role in cellular migration, axon guidance, and presynaptic development (14-16). It also regulates developing thymocyte survival, monocyte migration, osteoclast differentiation and function, cardiac muscle morphogenesis, and tumorigenesis (5, 8, 10-12). Ephrin-B1 is up‑regulated on reactive astrocytes and on macrophages and T cells found in atherosclerotic plaques (11, 17).

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. Shao, H. et al. (1994) J. Biol. Chem. 269:26606.
4. Fletcher, F.A. et al. (1994) Genomics 24:127.
5. Tanaka, M. et al. (2007) J. Cell Sci. 120:2179.
6. Tomita, T. et al. (2006) Mol. Neurodegen. 1:2.
7. Tanaka, M. et al. (2005) EMBO J. 24:3700.
8. Genet, G. et al. (2012) Circ. Res. 110:688.
9. Hashimoto, T. et al. (2007) Kidney Int. 72:954.
10. Yu, G. et al. (2006) J. Biol. Chem. 281:10222.
11. Sakamoto, A. et al. (2008) Clin. Sci. 114:643.
12. Cheng, S. et al. (2012) PLoS ONE 7:e32887.
13. Egawa, M. et al. (2003) J. Clin. Endocrinol. Metab. 88:4384.
14. Davy, A. et al. (2004) Genes Dev. 18:572.
15. Bush, J.O. and P. Soriano (2009) Genes Dev. 23:1586.
16. McClelland, A.C. et al. (2009) Proc. Natl. Acad. Sci. USA 106:20487.
17. Wang, Y. et al. (2005) Eur. J. Neurosci. 21:2336.

Publications for Ephrin-B1 (BT473)(1)

Publication using BT473

• Yu G, Luo H, Wu Y, Wu J EphrinB1 is essential in T-cell-T-cell co-operation during T-cell activation. J. Biol. Chem., 2004-10-22;279(53):55531-9. 2004-10-22 [PMID: 15502157] (Flow Cytometry, Mouse)

Bioinformatics

• Gene Symbol: Efnb1
• Uniprot:
  • Q544L9()