Overview
Co-IP is a classical in vivo protein-protein interaction technology developed based on the principle of Immunoprecipitation (IP). IP is a classical protein separation technique that leverages the specific recognition and binding of antibodies to target antigens, followed by isolation and purification of the antibody-antigen complex from complex biological samples using solid-phase carriers such as Protein A/G. The core of IP lies in “fishing out a single target protein”. It is widely applied in target protein enrichment, purity verification, post-translational modification analysis, and protein expression level detection, serving as a foundational tool in proteomics research. Co-IP is a powerful protein-protein interaction validation technology built upon the foundation of classical IP. While IP focuses on isolating a single target protein, Co-IP extends this principle to “fish out the target protein along with its interacting partners”. The workflow begins with the lysis of cells or tissues under non-denaturing conditions, carefully preserving endogenous protein-protein interaction complexes in their native state. The resulting lysate is then incubated with a target-specific antibody directed against the bait protein, enabling the co-capture of both the bait and its specifically associated interacting partners (prey proteins). Following stringent washes to eliminate non-specifically bound contaminants, the co-precipitated protein complexes are eluted under denaturing conditions. The eluate is subsequently analyzed by Western blot for validation of known interactors, or by LC-MS/MS for unbiased identification of novel interacting proteins. This approach enables indirect yet highly specific detection of proteins that associate with the target protein in its native cellular context, providing robust evidence for physiological protein-protein interactions.
Subcategories
Endogenous Co-IPEndogenous Co-IPEndogenous Co-IP refers to a technique that does not involve exogenous expression or tag fusion. Instead, it directly utilizes natively expressed proteins from cells or tissues, employing specific antibodies to perform immunoprecipitation, thereby validating protein-protein interactions under physiological conditions. Endogenous Co-IP can reflects authentic physiological interactions, preserves native PTMs, avoids overexpression artifacts.
>> View productsTagged Protein Co-IPTagged Protein Co-IPTagged Protein Co-IP refers to a technique where a target protein is overexpressed in cells with a specific epitope tag (Flag, HA, Myc, GFP, V5, etc.) via an exogenous expression system (plasmid transfection, viral infection, etc.). Anti-tag antibodies are then used to perform immunoprecipitation, validating interactions between the protein of interest and its binding partners.
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