If an antigen is injected into an animal, a number of antibody-producing cells will bind that antigen albeit with varying degrees of affinity, and so the antibody which appears in the bloodstream will have arisen from several clones of cells, that is it will be a polyclonal antibody. Different antibody molecules in a preparation of polyclonal antibody will bind to different parts of the macromolecular antigen and will do so with different binding affinities. The binding region recognized by any one antibody molecule is called an epitope. Most antibodies recognize particular surface structures in a protein rather than specific amino acid sequences (i.e. the epitopes are defined by the conformation of the protein antigen). A preparation of polyclonal antibodies will bind to many epitopes on the protein antigen. Whereas, Monoclonal antibodies are single clone of antibody-producing cells could be isolated, then all of the antibody produced from that clone would be identical; all antibody molecules in such a monoclonal antibody preparation would bind to the same antigen epitope. The problem is that if an individual antibody-producing cell is isolated and grown in culture, its descendants have a limited lifespan that severely limits their use for the routine preparation of monoclonal antibodies. Monoclonal antibodies produced using this technology are now common tools in research because of their very high specificity. For example, they can be used to locate particular molecules within cells or particular amino acid sequences within proteins. If they are first bound to an insoluble matrix, they are also extremely useful for binding to and hence purifying the particular molecule from crude cell extracts or fractions .They are also increasingly of use in medicine, both for diagnosis and as therapeutic tools, for example to inactivate bacterial toxins and to treat certain forms of cancer.
