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. 2007 Aug 3;359(3):655-9.
doi: 10.1016/j.bbrc.2007.05.152. Epub 2007 May 30.

Characterization of SynCAM surface trafficking using a SynCAM derived ligand with high homophilic binding affinity

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Characterization of SynCAM surface trafficking using a SynCAM derived ligand with high homophilic binding affinity

Christelle Breillat et al. Biochem Biophys Res Commun. .

Abstract

In order to better probe SynCAM function in neurons, we produced a fusion protein between the extracellular domain of SynCAM1 and the constant fragment of human IgG (SynCAM-Fc). Whether in soluble form or immobilized on latex microspheres, the chimera bound specifically to the surface of hippocampal neurons and recruited endogenous SynCAM molecules. SynCAM-Fc was also used in combination with Quantum Dots to follow the mobility of transfected SynCAM receptors at the neuronal surface. Both immobile and highly mobile SynCAM were found. Thus, SynCAM-Fc behaves as a high affinity ligand that can be used to study the function of SynCAM at the neuronal membrane.

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