Co-IP is a classic technology widely used for protein-protein interaction identification and validation. Based on the specific immunological interaction between the bait protein and its antibody, co-IP has become an effective and reliable method in detecting the physiological interaction between proteins.
The principle of the co-IP technique is as follows: Many intracellular protein-protein interactions are retained when cells are lysed under non-denaturing conditions. The bait protein, for example, protein X, can be captured by its specific antibody stabilized to agarose beads. If there is another protein, the prey protein, for example, protein Y, binds to protein X in vivo, the protein X – protein Y complex can then be precipitated together by the antibody. Subsequently, through the investigation of protein Y, we can confirm the protein X – protein Y interaction, or discover new interactors of protein X.
The advantage of this technology includes:
|Both the bait and prey proteins are in their native conformation in the co-IP assay.|
|The interaction between the bait and prey proteins happens in vivo with little to no external influence.|
The limitation of this technology lies in:
|Low affinity or transient interaction between proteins may not be detected.|
|The result of Co-IP could not determine whether the interaction is direct or indirect, since the possibility of involvement of additional proteins could not be ruled out.|
The result of co-IP reflects the physiological protein interactions in vivo. If researchers have predicted potential interactors, co-IP can be coupled with Western Blot assay as a way of protein interaction validation. If no prediction is made, co-IP can be coupled with Mass Spectrometry to identify new interactors.
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