Recombinant Mouse Ephrin-A2 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized recombinant rat EphA5 Fc Chimera at 2 µg/mL (100 µL/well) can bind rmEphrin-A2/Fc Chimera with a linear range of 0.16‑10 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Ephrin-A2 protein
>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
46 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
57 kDa, reducing conditions
Publications
Read Publications using 603-A2 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 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).
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Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
Shao, H. et al. (1995) J. Biol. Chem. 270:3467.
Cheng, H.-J. et al. (1994) Cell 79:157.
Kenmuir, C.L. et al. (2012) Anat. Rec. (Hoboken) 295:105.
Ohta, K. et al. (1997) Mech. Dev. 64:127.
Wada, N. et al. (2003) Dev. Biol. 264:550.
Gao, P.-P. et al. (1996) Proc. Natl. Acad. Sci. USA 93:11161.
Holmberg, J. et al. (2005) Genes Dev. 19:462.
Nakamoto, M. et al. (1996) Cell 86:755.
Symonds, A.C.E. et al. (2007) Eur. J. Neurosci. 25:744.
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