The BTB (B&barbelow;road complex, T&barbelow;ramtrack and B&barbelow;ric a Brac) domain is a versatile protein-protein interaction motif found in Eukaryotes and poxvirus. The human genome encodes 183 BTB-containing proteins, which function in an array of biological processes including protein degradation, cytoskeleton regulation, ion transport, and transcription regulation.Here we systematically investigate whether the BTB domains from a subset of BTB zinc finger transcription factors form homo- or heterotypic BTB-BTB associations using a size exclusion chromatography assay. Additionally, we used an in vitro FRET-based assay to evaluate the oligomerization capacity of the BTB domain from the transcription factor Kaiso. We found that the BTB domains from these transcription factors facilitate both homomeric and heteromeric associations, and may be able to oligomerize in the presence of a DNA template.