Recombinant Mouse Ephrin-B3 Fc Chimera Protein, CF Summary
Accession # O35393
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in 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.
Ephrin-B3, also known as Elk-L3, LERK8, Eplg8, NLERK-2, and EFL6, is an approximately 50 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-B3 preferentially interacts with receptors in the EphB family and also with EphA4. The binding of Ephrin-B3 to Eph proteins also triggers reverse signaling through Ephrin-B3 (1, 2). Mature mouse Ephrin-B3 consists of a 200 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 92 aa cytoplasmic domain (3, 4). Within the ECD, mouse Ephrin-B3 shares 96% and 98% aa sequence identity with human and rat Ephrin-B3, respectively. Ephrin-B3 is expressed on oligodendrocytes and neurons in the hippocampus and along the midline of the spinal cord (5-9). It is up-regulated in glioma and promotes tumor cell invasion and migration (10). Ephrin-B3 functions as a repulsive axon guidance molecule by inducing growth cone collapse, neurite retraction, and axon pruning (5-8). Its repulsive effect along the spinal cord midline restricts motor neuron axons to their ipsilateral sides, thereby maintaining the independence of voluntary left side/right side movements (8, 9). Ephrin-B3 plays a role in the regulation of excitatory synapse density and synaptic maturation (6, 11, 12). It also functions as a cellular receptor for Nipah virus (13) and can induce the migration of memory B cells (14).
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- Negrete, O.A. et al. (2006) PLoS Pathog. 2:e7.
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Citations for Recombinant Mouse Ephrin-B3 Fc Chimera Protein, CF
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.
Citations: Showing 1 - 5
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Guidance landscapes unveiled by quantitative proteomics to control reinnervation in adult visual system
Authors: N Vilallongu, J Schaeffer, AM Hesse, C Delpech, B Blot, A Paccard, E Plissonnie, B Excoffier, Y Couté, S Belin, H Nawabi
Nature Communications, 2022-10-13;13(1):6040.
Sample Types: Whole Tissue
Detection of Nipah and Hendra Viruses Using Recombinant Human Ephrin B2 Capture Virus in Immunoassays
Authors: M Yang, W Zhu, T Truong, B Pickering, S Babiuk, D Kobasa, L Banadyga
Sample Types: Cell Lysates
Applications: ELISA Capture
Identification and characterization of Nanobodies targeting the EphA4 receptor
Authors: L Schoonaert, L Rué, B Roucourt, M Timmers, S Little, L Chávez-Gut, M Dewilde, P Joyce, A Curnock, P Weber, J Haustraete, G Hassanzade, B De Stroope, L Van Den Bo, P Van Damme, R Lemmens, W Robberecht
J. Biol. Chem., 2017-05-19;292(27):11452-11465.
Sample Types: Whole Cells
EphB4 forward signalling regulates lymphatic valve development.
Authors: Zhang, Gu, Brady, John, Liang, Wei-Chin, Wu, Yan, Henkemeyer, Mark, Yan, Minhong
Nat Commun, 2015-04-13;6(0):6625.
Sample Types: Antibody
Applications: Enzyme Assay
Nipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering.
Authors: Liu Q, Bradel-Tretheway B, Monreal A, Saludes J, Lu X, Nicola A, Aguilar H
J Virol, 2014-11-26;89(3):1838-50.
Sample Types: Whole Cells
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