Catalog Number:

GT15025

Product Type:

Affinity Purified

Immunogen Sequence:

Recombinant mouse Ephrin-A2 extracellular domain

Host:

Goat

Reactivity:

Mouse, Rat

Applications:

Immunohistochemistry, Western Blot, ELISA

Description:

Although ephrins form a high-affinity multivalent complex with their receptors present on axons, axons can be rapidly repelled rather than being bound. Ephrin-A2 forms a stable complex with the metalloproteinase Kuzbanian (ADAM10), involving interactions outside the cleavage region and the protease domain. Eph receptor binding triggered ephrin-A2 cleavage in a localized reaction specific to the cognate ligand. The cleavage-inhibiting mutation in ephrin-A2 delayed axon withdrawal. Studies reveal mechanisms for protease recognition and control of cell surface proteins, and, for ephrin-A2, they may provide a means for efficient axon detachment and termination of signaling.

Reference:

Aasheim, H.-C.; Pedeutour, F.; Grosgeorge, J.; Logtenberg, T. :
Cloning, chromosomal mapping, and tissue expression of the gene encoding the human Eph-family kinase ligand ephrin-A2. Biochem. Biophys. Res. Commun. 252: 378-382, 1998.

Cerretti, D. P.; Nelson, N. :
Characterization of the genes for mouse LERK-3/Ephrin-A3 (Epl3), mouse LERK-4/Ephrin-A4 (Epl4), and human LERK-6/Ephrin-A2 (EPLG6): conservation of intron/exon structure. Genomics 47: 131-135, 1998.

Hattori, M.; Osterfield, M.; Flanagan, J. G. :
Regulated cleavage of a contact-mediated axon repellent. Science 289: 1360-1365, 2000.