Recombinant Human Ephrin-A3 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to compete with Biotinylated Recombinant Human Ephrin‑A3 Fc Chimera (Catalog # BT359) for binding to immobilized recombinant mouse Eph-A6 Fc Chimera in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human Ephrin-A3 protein
Human Ephrin-A3 (Asn31-Ser209) Accession # AAA52368
>90%, 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
Binding Activity
Theoretical MW
47.7 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
60-70 kDa, reducing conditions
Publications
Read Publications using 359-EA 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
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Ephrin-A3 Fc Chimera Protein, CF
EFL2
EFL-2
EFNA3
Ehk1-L
EPH-related receptor tyrosine kinase ligand 3
EphrinA3
Ephrin-A3
EPLG3EHK1 ligand
LERK3
LERK3LERK-3
ligand of eph-related kinase 3
Background
Ephrin‑A3, also known as EHK1‑L, EFL‑2, and LERK‑3, is an approximately 25 kDa member of the Ephrin‑A family of GPI‑anchored ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. Ephrin‑A ligands are structurally related to the extracellular domains of the transmembrane Ephrin‑B ligands. Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. Ephrin‑A3 preferentially interacts with receptors in the EphA family (1, 2). Ephrin‑A3 is an unusual Ephrin‑A molecule in its dependence on heparan sulfate binding for full activity (3). Mature human Ephrin‑A3 shares 92% aa sequence identity with mouse and rat Ephrin‑A3 (4). Its expression is restricted to discreet locations during the early development of multiple tissues (5). Ephrin‑A3 expression can be up‑ or down‑regulated by hypoxia in the hippocampus or vascular endothelial cells, respectively (6, 7). Ephrin‑A3 down‑regulation contributes to hypoxia‑induced endothelial cell chemotaxis, proliferation, and tubule formation (7). Its interaction with EphA receptors induces neurite growth cone collapse and the repulsion of migrating axons (8‑10). This activity is important for the accurate pathfinding of migrating axons during CNS development (10). Astrocyte‑expressed Ephrin‑A3 activates EphA4 on hippocampal neurons to regulate dendritic spine morphology and long term potentiation (8, 11, 12). The same interaction induces reverse signaling through Ephrin‑A3 to regulate glutamate uptake by the astrocyte and the availability of glutamate in the synapse (11, 12). Astrocyte‑expressed Ephrin‑A3 also interacts with EphA7 to inhibit the proliferation of neural progenitor cells (13).
Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
Irie, F. et al. (2008) Proc. Natl. Acad. Sci. 105:12307.
Davis, S. et al. (1994) Science 266:816.
Duffy, S.L. et al. (2006) Gene Expr. Patterns 6:719.
Pulkkinen, K. et al. (2008) FEBS Lett. 582:2397.
Fasanaro, P. et al. (2008) J. Biol. Chem. 283:15878.
Murai, K.K. et al. (2003) Nat. Neurosci. 6:153.
Stein, E. et al. (1999) J. Neurosci. 19:8885.
Rudolph, J. et al. (2010) Cell Adh. Migr. 4:400.
Filosa, A. et al. (2009) Nat. Neurosci. 12:1285.
Carmona, M.A. et al. (2009) Proc. Natl. Acad. Sci. 106:12524.
Jiao, J. et al. (2008) Proc. Natl. Acad. Sci. 105:8778.
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