Recombinant Mouse Ephrin-B1 Fc Chimera Protein, CF

R&D Systems | Catalog # 473-EB

R&D Systems
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Key Product Details

  • R&D Systems NS0-derived Recombinant Mouse Ephrin-B1 Fc Chimera Protein (473-EB)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

NS0

Accession Number

Structure / Form

Disulfide-linked homodimer

Applications

Binding Activity
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Product Specifications

Source

Mouse myeloma cell line, NS0-derived mouse Ephrin-B1 protein
Mouse Ephrin-B1
(Lys30-Ser229)
Accession # AAA53231
IEGRMD Human IgG1
(Pro100-Lys330)
6-His tag
N-terminus C-terminus

Purity

>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.

N-terminal Sequence Analysis

Lys30

Predicted Molecular Mass

49.2 kDa (monomer)

SDS-PAGE

60 kDa, reducing conditions

Activity

Measured by its binding ability in a functional ELISA.
Immobilized recombinant mouse EphB3 Fc Chimera at 2 µg/mL (100 µL/well) can bind Recombinant Mouse Ephrin-B1 Fc Chimera with a linear range of 0.01-0.5 ng/mL.

Formulation, Preparation, and Storage

473-EB
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution

Reconstitute at 100 μg/mL in sterile PBS.


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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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Ephrin-B1

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).

References

  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.

Alternate Names

Cek5-L, EFL-3, EFNB1, ELK-L, EphrinB1, LERK-2, STRA-1

Entrez Gene IDs

1947 (Human); 13641 (Mouse); 25186 (Rat)

Gene Symbol

EFNB1

UniProt

Additional Ephrin-B1 Products

Product Documents for Recombinant Mouse Ephrin-B1 Fc Chimera Protein, CF

Certificate of Analysis

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Product Specific Notices for Recombinant Mouse Ephrin-B1 Fc Chimera Protein, CF

For research use only

Related Research Areas

Citations for Recombinant Mouse Ephrin-B1 Fc Chimera Protein, CF

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