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

In the presence of heparin, ihog forms a dimer.

Native molecular weight was determined by size exclusion chromatography of purified protein.

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

In the presence of heparin, ihog forms a dimer.

Molecular weight of purified ihog estimated by analytical ultracentrifugation and calculation of sedimentation coefficient.

Coexpression of the N-terminal hh signaling domain reduces the ihog-ihog interaction.

Source was cell medium of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

Deletion of ihog FnIII-2 domain reveals ihog homophilic trans-binding.

Source was larval wing discs of transgenic fly line; proteins produced from transgenic constructs.