Recombinant Human Ephrin-B3 Fc Chimera Protein, CF Summary
Accession # NP_001397
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 400 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 human Ephrin‑B3 consists of a 199 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 93 aa cytoplasmic domain (3, 4). Within the ECD, human Ephrin‑B3 shares 96% and 97% aa sequence identity with mouse 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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Citations for Recombinant Human Ephrin-B3 Fc Chimera Protein, CF
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Citations: Showing 1 - 2
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Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus
Authors: ED Laing, CK Navaratnar, S Cheliout D, SR Petzing, Y Xu, SL Sterling, GA Marsh, LF Wang, M Amaya, DB Nikolov, R Cattaneo, CC Broder, K Xu
Proc. Natl. Acad. Sci. U.S.A., 2019-09-23;0(0):.
Species: Virus - Henipavirus
Sample Types: Recombinant Protein
Applications: Coprecipitation Assay
The composition of EphB2 clusters determines the strength in the cellular repulsion response.
Authors: Schaupp A, Sabet O, Dudanova I, Ponserre M, Bastiaens P, Klein R
J Cell Biol, 2014-01-27;204(3):409-22.
Sample Types: Whole Cells
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