Immunoprecipitation (IP) is a small-scale affinity purification technique used to isolate and concentrate a particular antigen from a sample solution, which may contain numerous other proteins. This is achieved by using an antibody that recognizes the target protein and is immobilized to a solid support like magnetic particles or agarose resin.
There are several different approaches, including the traditional (classical) method, oriented affinity method and direct affinity method. The traditional method of IP involves incubating the antibody with a sample, then binding it to Protein A or G agarose. However, this can lead to the target protein getting contaminated with the IP antibody, complicating subsequent analyses.
The oriented affinity technique uses Protein A or G beads as anchors, crosslinking the IP antibody to them. This prevents the antibody and target protein from being eluted together. In another approach, the direct affinity method attaches the IP antibody directly to a chemically activated base.1
IP offers several benefits for scientists, such as detecting protein activation states, post-translational modifications, estimating molecular weights of proteins, and investigating protein-protein and protein-nucleic acid interactions.
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References:
Kaboord, B., & Perr, M. (2008). Isolation of proteins and protein complexes by immunoprecipitation. Methods in molecular biology (Clifton, N.J.), 424, 349–364. https://doi.org/10.1007/978-1-60327-064-9_27
