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

Interaction of kay and Jra was observed as a slower moving complex on the EMSA gel distinct from the complex formed by either kay or Jra alone and appears to have a higher affinity fo the AP-1 site used as a probe.

Interaction in vitro; fluorescence donor produced as a recombinant fusion protein in bacterial system and labeled in vitro; fluorescence acceptor produced as a recombinant fusion protein in bacterial system and labeled in vitro.

Dissociation constant of Kd=14nM.

Interactions between bZIP proteins were quantified in vitro using a solution FRET assay at 4oC, 21oC and 37oC. Only interactions at 21oC with Kd < 5000 nm were curated by FlyBase.

Interaction in vitro; fluorescence donor produced as a recombinant fusion protein in bacterial system and labeled in vitro; fluorescence acceptor produced as a recombinant fusion protein in bacterial system and labeled in vitro.

Dissociation constant of Kd=12nM.

Interactions between bZIP proteins were quantified in vitro using a solution FRET assay at 4oC, 21oC and 37oC. Only interactions at 21oC with Kd < 5000 nm were curated by FlyBase.

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast GAL4-BD/GAL4-AD