No results obtained: Gln21 predicted, sequencing might be blocked
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Efna5
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
48.4 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
57-60 kDa, reducing conditions
Publications
Read Publications using 7396-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
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 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-A5 Fc Chimera Protein, CF
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 mouse Ephrin‑A5 shares 98.9% and 99.5% aa sequence identity with human and rat Ephrin‑A5 (4). Alternate splicing of mouse Ephrin‑A5 generates a short isoform that lacks 27 amino acids in the juxtamembrane region. The short isoform retains the ability to bind EphA3 and inhibit neurite extension (5). Ephrin‑A5 is expressed in multiple tissues during development, particularly in the brain (6, 7). It can exert repulsive or attractive effects on migrating neurons in the developing brain and motor column of the spinal cord (7‑11). Ephrin‑A5 repels migrating axons by inducing growth cone collapse and neurite retraction and by inhibiting the neurotrophic effects of NGF and BDNF (3, 12, 13). It interacts in cis with EphA3 on retinal axon growth cones which reduces axonal sensitivity to Ephrin‑A5 in trans (14). In the adult, Ephrin‑A5 is expressed on hippocampal neurons and astrocytes and induces the development of hippocampal synapses (10, 15, 16). It supports the proliferation of neural progenitors and the survival of newly differentiated neurons (15). Ephrin‑A5 functions as a tumor suppressor and its normal function in inhibiting EGFR signaling is compromised by its down‑regulation in glioma (17). Ephrin A5 is also down‑regulated in prostate cancer (18). Ephrin‑A5 is expressed by muscle precursor cells and interacts with EphA4 to restrict their migration to the correct locations during forelimb morphogenesis (19).
Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
Himanen, J.-P. et al. (2004) Nat. Neurosci. 7:501.
Flenniken, A.M. et al. (1996) Dev. Biol. 179:382.
Lai, K.-O. et al. (1999) FEBS Lett. 458:265.
Deschamps, C. et al. (2010) BMC Neurosci. 11:105.
Cooper, M.A. et al. (2009) Dev. Neurobiol. 69:36.
Frisen, J. et al. (1998) Neuron 20:235.
Zimmer, G. et al. (2008) Eur. J. Neurosci. 28:62.
Otal, R. et al. (2006) Neuroscience 141:109.
Eberhart, J. et al. (2004) J. Neurosci. 24:1070.
Munoz, L.M. et al. (2005) Dev. Biol. 283:397.
Meier, C. et al. (2011) PLoS ONE 6:e26089.
Carvalho, R.F. et al. (2006) Nat. Neurosci. 9:322.
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