Dscam1-Fc fusion protein was recovered from conditioned medium and coupled to protein-A-coated fluorescent beads. Homophilic Dscam1 interaction was inferred from bead aggregation under fluorescence microscopy.

Dscam1 exhibits isoform-specific homophilic binding.

Interaction in vitro; protein derived from conditioned medium of transfected S2 cells.

Fc-tagged Dscam1 was collected from conditioned S2 cell medium and coupled to fluorescent beads. Beads were then incubated with live, transfected S2 cells expressing Dscam1. Binding of beads to the cell surface was detected by fluorescence microscopy and used to infer homophilic Dscam1 interaction.

Dscam1 exhibits isoform-specific homophilic binding.

Interaction in vitro; bait derived from transfected S2 cells; prey derived from conditioned medium of transfected S2 cells.

Fc-tagged Dscam1 was collected from S2 cell conditioned medium, and incubated with a separate cell extract from S2 cells expressing FLAG-tagged Dscam1.

Dscam1 exhibits isoform-specific homophilic binding.

Interaction in vitro; bait derived from conditioned medium of transfected S2 cells; prey derived from transfected S2 cell line extract.

Source was live Cos cells; proteins produced from transfected constructs.

Physical interaction of proteins expressed on the surface of cells and beads is inferred from the aggregation of live cells with beads.

Fc-tagged Dscam1 was collected from S2 cell conditioned medium, and incubated with a separate cell extract from S2 cells expressing FLAG-tagged Dscam1.

Interaction in vitro; bait derived from conditioned medium of transfected S2 cells; prey derived from transfected S2 cell line extract.

Dscam1 dimerizes. It does not interact with Dscam2.

Interaction in vitro; bait derived from conditioned media of transfected S2 cell line; prey derived from conditioned media of transfected S2 cell line.

Homodimers of wildtype isoforms 7.27.25 and 3.31.8 observed. Homodimers were not observed with isoforms carrying chimeric Ig2 domains.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus system.

A conserved homodimer geometry was observed for 12 different isoforms.