Recombinant Mouse Ephrin-A2 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Ephrin-A2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit proliferation of PC-3 human prostate cancer cells. The ED 50 for this effect is 5-30 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Ephrin-A2 protein
Mouse Ephrin-A2 (Glu23-Asn184) Accession # P52801 IEGRMDP Mouse IgG 2A (Glu98-Lys330) N-terminus C-terminus
Accession #
N-terminal Sequence
Glu23
Structure / Form
Disulfied-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Efna2
Purity
>90%, by SDS-PAGE with silver staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
46 kDa.
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
52-61 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 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 250 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 Mouse Ephrin-A2 Fc Chimera Protein, CF

  • Cek7-L
  • EFNA2
  • ELF-1
  • EPH-related receptor tyrosine kinase ligand 6
  • EphrinA2
  • Ephrin-A2
  • EPLG6HEK7 ligand
  • HEK7-L
  • HEK7-ligand
  • LERK6
  • LERK6LERK-6
  • ligand of eph-related kinase 6

Background

Ephrin-A2, also known as ELF-1, HEK7-L, LERK-6, and EPLG6, is an approximately 20 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-A2 preferentially interacts with receptors in the EphA family (1, 2). Mouse Ephrin-A2 is synthesized with a 20 amino acid (aa) signal peptide, a 164 aa mature chain, and a 25 aa C-terminal propeptide which is removed prior to GPI linkage of Ephrin-A2 to the membrane (3, 4). It shares 93% and 100% aa sequence identity with human and rat Ephrin-A2, respectively. Ephrin-A2 is expressed in discrete regions of the developing nervous system and limb buds (4-7). Its distribution complements the pattern of Eph receptor expression, and this plays an important role in tissue morphogenesis (7-9). Ephrin-A2 exerts an axon repulsive signal which is important for the accurate pathfinding of retinal ganglion cell axons to the tectum and hippocampal axons to the lateral septum (8, 10). Its up-regulation in astrocytes at sites of optic nerve damage may prevent re-innervation by retinal ganglion cells (11). Ephrin-A2 is also expressed on neural progenitor cells in the subventricular zone (SVZ). It interacts with EphA7, triggering reverse signaling through Ephrin-A2 and inhibition of progenitor cell proliferation (9). In the developing limbs, Ephrin-A2 regulates cartilage morphogenesis and the projection of motoneuron axons (6, 7, 12).
  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. Shao, H. et al. (1995) J. Biol. Chem. 270:3467.
  4. Cheng, H.-J., and J.G. Flanagan (1994) Cell 79:157.
  5. Kenmuir, C.L. et al. (2012) Anat. Rec. (Hoboken) 295:105.
  6. Ohta, K. et al. (1997) Mech. Dev. 64:127.
  7. Wada, N. et al. (2003) Dev. Biol. 264:550.
  8. Gao, P.-P. et al. (1996) Proc. Natl. Acad. Sci. USA 93:11161.
  9. Holmberg, J. et al. (2005) Genes Dev. 19:462.
  10. Nakamoto, M. et al. (1996) Cell 86:755.
  11. Symonds, A.C.E. et al. (2007) Eur. J. Neurosci. 25:744.
  12. Eberhart, J. et al. (2000) Dev. Neurosci. 22:237.

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Bioinformatics

Gene Symbol Efna2
Entrez
Uniprot