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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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
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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