Immunopipitaatio

Immunopipitaatio is a technique used in immunology and molecular biology to isolate and purify specific antigens or antibodies from a complex mixture. It relies on the principle of immunoprecipitation, where an antibody specifically binds to its target antigen. This antigen-antibody complex can then be precipitated out of solution using various methods, typically by adding a secondary antibody or a protein A or G resin that binds to the first antibody.

The process begins by incubating a sample containing the antigen of interest with a specific antibody. This antibody, known as the primary antibody, is designed to recognize and bind to a particular epitope on the antigen. After a period of incubation to allow for binding, the mixture is treated to precipitate the formed antigen-antibody complex. Common precipitation methods involve using magnetic beads or agarose beads coated with reagents that bind to the primary antibody. These beads, along with the bound complex, can then be easily separated from the rest of the solution through centrifugation or magnetic separation.

Following precipitation, the isolated complex is washed to remove any non-specifically bound molecules. Finally, the antigen or antibody is eluted from the antibody, often by altering the pH or using a competitive ligand. The eluted material can then be analyzed using various techniques, such as Western blotting, mass spectrometry, or enzyme-linked immunosorbent assays (ELISA), to confirm the identity and purity of the isolated substance. Immunopipitaatio is a valuable tool for studying protein-protein interactions, identifying specific proteins in cellular lysates, and purifying antibodies for therapeutic or diagnostic purposes.