Recombinant Human Ephrin-B2 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human EphB2 Fc Chimera (Catalog # 5189-B2) is coated at 2 μg/mL, Recombinant Human Ephrin‑B2 Fc Chimera binds with an apparent Kd <0.1 nM. Also measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neuron.
Source
Mouse myeloma cell line, NS0-derived human Ephrin-B2 protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
48.8 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
58-66 kDa, reducing conditions
Publications
Read Publications using 7397-EB in the following applications:
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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 300 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Ephrin-B2 Fc Chimera Protein, CF
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 human Ephrin-B2 consists of a 202 amino acid (aa) extracelluar domain (ECD), a 21 aa transmembrane segment, and an 83 aa cytoplasmic domain (3). Within the ECD, human Ephrin-B2 shares 97% aa sequence identity with mouse and rat Ephrin-B2. Ephrin-B2 is expressed presynaptically on neurons (4, 5). It promotes presynaptic development, EphB2 shedding, axonal growth cone collapse, and neurite repulsion, and also regulates inflammatory and neuropathic pain (4-6). Ephrin-B2 is expressed by vascular mural cells and arterial vascular and lymphatic endothelium (7, 8). 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 (7-9). Ephrin-B2 plays a role in the immune response by mediating monocyte extravasation and T cell costimulation (10, 11). It is up‑regulated in invasive cancers and promotes tumor cell migration, invasion, and tumor angiogenesis (12-14). It functions as a cellular entry receptor for Hendra and Nipah viruses (15). Ephrin-B2 is also important for the separation of the urinary and intestinal tracts during development (16).
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Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
Cerretti, D.P. et al. (1995) Mol. Immunol. 32:1197.
McClelland, A.C. et al. (2009) Proc. Natl. Acad. Sci. 106:20487.
Zhao, J. et al. (2010) Mol. Pain 6:77.
Lin, K.-T. et al. (2008) J. Biol. Chem. 283:28969.
Foo, S.S. et al. (2006) Cell 124:161.
Wang, Y. et al. (2010) Nature 465:483.
Sawamiphak, S. et al. (2010) Nature 465:487.
Pfaff, D. et al. (2008) J. Cell Sci. 121:3842.
Yu, G. et al. (2003) J. Immunol. 171:106.
Meyer, S. et al. (2005) Int. J. Oncol. 27:1197.
Nakada, M. et al. (2010) Int. J. Cancer 126:1155.
Liu, W. et al. (2004) Br. J. Cancer 90:1620.
Bonaparte, M.I. et al. (2005) Proc. Natl. Acad. Sci. 102:10652.
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