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

In size-exclusion chromatography, the CTCF N-terminal domain had a hydrodynamic mass of ~250 kDa that was greater than the 45 kDa predicted for the monomer.

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

In cross-linking study, the CTCF N-terminal domain had a hydrodynamic mass much greater than the 45 kDa predicted for the monomer. Efficient cross-linking suggests that CTCF multimers observed in size-exclusion chromatography do not represent non-specific aggregates.

Glutaraldehyde cross-linking.

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

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

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

Estimated molecular weight from cross-linking and electrophoresis is consistent with a dimer.

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

Estimated molecular weight from light scattering is consistent with a tetramer.

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

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

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/VP16-AD. The N-terminal dimerization domain of CTCF is able to homodimerize and interact with the proximal N-terminal dimerization domain.