Recombinant Mouse Ephrin-A3 Fc Chimera Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Ephrin-A3 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit proliferation of PC‑3 human prostate cancer cells. The ED₅₀ for this effect is 15-75 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse Ephrin-A3 protein
  

  Mouse Ephrin-A3 (Gln23-Gly206) Accession # NP_034238	IEGRMDP	Mouse IgG2A (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: NP_034238
• N-terminal Sequence: Gln23 predicted: No results obtained, sequencing might be blocked
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >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 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: 60-66 kDa, reducing conditions

Packaging, Storage & Formulations

• 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.
• 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 Mouse 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 (1, 2). 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 mouse Ephrin‑A3 shares 92% and 100% aa sequence identity with human and rat Ephrin‑A3, respectively (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).

1. Pasquale, E.B. (2008) Cell 133:38.
2. Astin, J.W. et al. (2010) Nat. Cell Biol. 12:1194
3. Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
4. Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
5. Irie, F. et al. (2008) Proc. Natl. Acad. Sci. 105:12307.
6. Ceretti, D.P. and N. Nelson (1998) Genomics 47:131.
7. Duffy, S.L. et al. (2006) Gene Expr. Patterns 6:719.
8. Pulkkinen, K. et al. (2008) FEBS Lett. 582:2397.
9. Fasanaro, P. et al. (2008) J. Biol. Chem. 283:15878.
10. Murai, K.K. et al. (2003) Nat. Neurosci. 6:153.
11. Stein, E. et al. (1999) J. Neurosci. 19:8885.
12. Rudolph, J. et al. (2010) Cell Adh. Migr. 4:400.
13. Filosa, A. et al. (2009) Nat. Neurosci. 12:1285.
14. Carmona, M.A. et al. (2009) Proc. Natl. Acad. Sci. 106:12524.
15. Jiao, J. et al. (2008) Proc. Natl. Acad. Sci. 105:8778.

Bioinformatics

• Uniprot:
  • NP_034238()