Bimolecular Fluorescence Complementation (BiFC) Service

Bimolecular Fluorescence Complementation (BiFC) technology is based on the principle of protein fragment complementation and is used to study protein-protein interactions. The principle involves splitting a fluorescent protein (such as Green Fluorescent Protein GFP, Yellow Fluorescent Protein YFP, etc.) into two complementary but non-fluorescent fragments (such as N-terminal and C-terminal fragments), which are then fused to the proteins of interest (Protein A and Protein B) for co-expression in cells. When Protein A interacts with Protein B within the cell, the fluorescent protein fragments are brought into proximity and reassemble into a complete fluorescent protein, generating a fluorescent signal that can be visualized under a microscope, providing direct evidence of protein interaction.

• Detection in living cells: Allows direct observation of protein interactions in physiological conditions, preserving spatiotemporal dynamic information.
• High specificity: Fluorescent signals only appear when target proteins interact, reducing false positives and improving detection specificity.
• Detection of weak or transient interactions: Sensitive to low-affinity, brief interactions, capable of revealing interactions difficult to detect by traditional methods.
• Visualization of subcellular localization: Simultaneously reveals the subcellular localization of the interaction. Applicable to various biological systems: Can be used in mammalian cells, plant cells, yeast, and other model organisms.