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=233nM.
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=510nM.
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 cell extract of S2 cell line; bait produced from transfected construct; prey produced from endogenous gene.
Source was nuclear extract of Kc cell line; bait produced from endogenous gene; prey produced from endogenous gene.
Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.
Source was larval eye discs of transgenic fly line; proteins produced from tagged transgenic construct.
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
