Cell, Volume 130 Supplemental Data A Vast Repertoire of Dscam Binding Specificities Arises from Modular Interactions of Variable Ig Domains

The binding properties of Dscam isoforms containing Ig2.7, Ig3.27 and highly-related Ig7 domains are shown in four different binding assays. The table outlines the properties of each binding assay to indicate 1) sensitivity (as determined by whether heterophilic binding can be detected between isoforms 7.27.25 and 7.27.26), 2) whether the assay is readily quantitative, 3) whether the assay requires protein purification, and 4) the number of binding experiments that can be conducted per day in our hands. Representative binding data for these isoforms in each assay are shown (Matthews et al., 2007; Wojtowicz et al., 2004)(J.J. Flanagan and S.L.Z, unpublished observations). F.L., full length. Figure S2. Detection of Homophilic Binding Requires Clustering of Dscam Molecules. (A) Immunoprecipitation assay to assess Dscam homophilic binding. Purified Dscam-Fc (bound to protein G sepharose) was used as receptor protein to pull-down purified Dscam-His ligand protein. Pull