Recombinant Human Ephrin-A5 Fc Chimera Biotinylated Protein

• Reactivity: Hu
• Applications: Binding Activity

Recombinant Human Ephrin-A5 Fc Chimera Biotinylated Protein Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized recombinant mouse EphA3 Fc Chimera at 2 µg/mL (100 µL/well) can bind Biotinylated Recombinant Human Ephrin-A5 Fc Chimera with a linear range of 0.078‑5 ng/mL.
  Optimal dilutions should be determined by each laboratory for each application.
• Source: Mouse myeloma cell line, NS0-derived human Ephrin-A5 protein
  

  Human Ephrin-A5 (Gln21 - Asn203) Accession # P52803	IEGRMD	Human IgG1 (Pro100 - Lys330)	6-His tag
  N-terminus			C-terminus

• Accession #: P52803
• N-terminal Sequence: No results obtained: Gln21 predicted
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: EFNA5
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 48.6 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: 50-55 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 with BSA as a carrier protein.
• 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-A5 Fc Chimera Biotinylated Protein

• AF1
• AL-1
• EFL-5
• EFNA5
• EPH-related receptor tyrosine kinase ligand 7
• EphrinA5
• Ephrin-A5
• EPLG7
• GLC1M
• LERK-7
• LERK7EFL5
• RAGS

Background

Ephrin‑A5, also known as AL‑1, RAGS, and LERK‑7, 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‑A5 preferentially interacts with receptors in the EphA family but also with EphB2 (3). Mature human Ephrin‑A5 shares 99.5% aa sequence identity with mouse and rat Ephrin‑A5, respectively (4). Ephrin‑A5 is expressed in multiple tissues during development, particularly in the brain (5, 6). It can exert repulsive or attractive effects on migrating neurons in the developing brain and motor column of the spinal cord (6 ‑ 10). Ephrin‑A5 repels migrating axons by inducing growth cone collapse and neurite retraction and by inhibiting the neurotrophic effects of NGF and BDNF (3, 11, 12). It interacts in cis with EphA3 on retinal axon growth cones which reduces axonal sensitivity to Ephrin‑A5 in trans (13). In the adult, Ephrin‑A5 is expressed on hippocampal neurons and astrocytes and induces the development of hippocampal synapses (9, 14, 15). It supports the proliferation of neural progenitors and the survival of newly differentiated neurons (14). Ephrin‑A5 also functions as a tumor suppressor (16). Its normal function in inhibiting EGFR signaling is compromised by its down‑regulation in glioma (16). Ephrin‑A5 is also expressed by muscle precursor cells and interacts with EphA4 to restrict their migration to the correct locations during forelimb morphogenesis (17).

1. Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
2. Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
3. Himanen, J.-P. et al. (2004) Nat. Neurosci. 7:501.
4. Winslow, J.W. et al. (1995) Neuron 14:973.
5. Deschamps, C. et al. (2010) BMC Neurosci. 11:105.
6. Cooper, M.A. et al. (2009) Dev. Neurobiol. 69:36.
7. Frisen, J. et al. (1998) Neuron 20:235.
8. Zimmer, G. et al. (2008) Eur. J. Neurosci. 28:62.
9. Otal, R. et al. (2006) Neuroscience 141:109.
10. Eberhart, J. et al. (2004) J. Neurosci. 24:1070.
11. Munoz, L.M. et al. (2005) Dev. Biol. 283:397.
12. Meier, C. et al. (2011) PLoS ONE 6:e26089.
13. Carvalho, R.F. et al. (2006) Nat. Neurosci. 9:322.
14. Hara, Y. et al. (2010) Stem Cells 28:974.
15. Akaneya, Y. et al. (2010) PLoS ONE 5:e12486.
16. Li, J.-J. et al. (2009) Oncogene 28:1759.
17. Swartz, M.E. et al. (2001) Development 128:4669.

Publications for Ephrin-A5 (BT374)(1)

Publication using BT374

• Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (Bioassay, Human)

Bioinformatics

• Gene Symbol: EFNA5
• Uniprot:
  • P52803()