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Bimolecular Fluorescence Complementation (BiFC) is an imaging technique for visualizing protein-protein interactions in living cells. The principle involves splitting a fluorescent protein (e.g., YFP, Venus, GFP) into N-terminal and C-terminal non-fluorescent fragments, each fused to a candidate interacting protein (Bait and Prey). When Bait and Prey physically interact within the cell, the two fluorescent fragments are brought into close proximity and refold to reconstitute the intact fluorescent protein structure, generating a detectable fluorescent signal. This signal appears exclusively at the subcellular location where the interaction occurs, enabling simultaneous qualitative detection and spatial localization of the interaction. However, due to its irreversibility, BiFC is not suitable for studying dynamic interactions.