To monitor ternary complex formation mediated by FerroTACs, we leveraged native gel electrophoresis assay, a methodology recently validated to assess VHL dimerization in homo-PROTACs. This in vitro approach serves as a rapid semi-qualitative tool to evaluate homo-FerroTAC activity in promoting stable ternary protein complexes. The technique is userfriendly, suitable for higher throughput, and requires lower protein quantities compared to other biophysical methods. The recombinant VCB protein complex (VHL:ElonginC:ElonginB) was incubated with the corresponding Homo-PROTACs (CM11, AS1, cisAS1, AS2) for 30 minutes at room temperature, followed by non-denaturing gel electrophoresis. Ternary complex formation was indicated by an upward shift in the protein band on the gel. Both AS1 and AS2, similarly to reference compound CM11, induced formation of an up-shifted protein band, consistent with the formation of stable ternary complexes VCB2:PROTAC (Figure ). Competitive assays were conducted to unequivocally assign the migrating bands to the expected ternary complexes by pre-incubating VCB with increasing concentrations of the high-affinity inhibitor VH298 (Figure ) or PROTAC AS2 (Figure ).