Recombinant Mouse Ephrin-B2 Fc Chimera Biotinylated Protein

Catalog # Availability Size / Price Qty
BT496
R&D Systems Recombinant Proteins and Enzymes
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Citations (3)
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Recombinant Mouse Ephrin-B2 Fc Chimera Biotinylated Protein Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
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 #
N-terminal Sequence
Analysis
Arg27
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
49.6 kDa (monomer)
SDS-PAGE
60-65 kDa, reducing conditions

Product Datasheets

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BT496

BT496

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
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.
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Background: Ephrin-B2

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).

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. 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.
Entrez Gene IDs
1948 (Human); 13642 (Mouse); 30219 (Zebrafish)
Alternate Names
EFNB2; ELF-2; ephrin B2; EphrinB2; Ephrin-B2; EPLG5; HTKL; Htk-L; LERK5; LERK-5; NLERK-1

Citations for Recombinant Mouse Ephrin-B2 Fc Chimera Biotinylated Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Fc-Based Recombinant Henipavirus Vaccines Elicit Broad Neutralizing Antibody Responses in Mice
    Authors: Y Li, R Li, M Wang, Y Liu, Y Yin, X Zai, X Song, Y Chen, J Xu, W Chen
    Viruses, 2020-04-23;12(4):.
    Species: Mouse
    Sample Types: Protein
    Applications: Bioassay
  2. Optimization and Diagnostic Evaluation of Monoclonal Antibody-based Blocking ELISA Formats for Detection of Neutralizing Antibodies to Hendra Virus in Mammalian Sera
    Authors: A Di Rubbo, L McNabb, R Klein, JR White, A Colling, DS Dimitrov, CC Broder, D Middleton, RA Lunt
    J. Virol. Methods, 2019-09-09;274(0):113731.
    Species: Virus - Hendra
    Sample Types: Recombinant Protein
    Applications: Bioassay, ELISA Detection
  3. Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1.
    Authors: Moza B, Varma AK, Buonpane RA, Zhu P, Herfst CA, Nicholson MJ, Wilbuer AK, Seth NP, Wucherpfennig KW, McCormick JK, Kranz DM, Sundberg EJ
    EMBO J., 2007-02-01;26(4):1187-97.
    Species: Mouse
    Sample Types:
    Applications: Surface Plasmon Resonance

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