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Antigens such as toxin-protein conjugates display epitopes, which the antibodies recognize through their combining sites, known as the paratope. Immunization of one species with antibodies from another species can yield several types of antibodies. For example, immunization of rabbits with mouse antibodies can result in rabbit antibodies directed against species (mouse)-specific epitopes (xenotypic antibodies), as well as antibodies directed against epitopes specific to individual clones within the mouse (idiotypic antibodies). The original antibody directed against the toxin is termed Ab1, while the anti-idiotypes are termed Ab2. Ab2 bind to epitopes (idiotopes) of the original antibody. Since the variable regions are involved in antigen binding, the attachment of Ab2 there can, in some cases, interfere with the antigen-antibody binding. Not all Ab2 can interfere with antigen binding, and the anti-idiotypes are further subdivided into groups that do not (Ab2α) or do (Ab2β, Ab2γ) cause such interference. The Ab2α recognize idiotopes distal from the antigen binding site (e.g., distal from the paratope). The Ab2β and Ab2γ anti-idiotypes bind either close to, or within the paratope. These two groups are separated based upon whether they carry an internal image of the original antigen (Ab2β), and those which do not (Ab2γ). Ab2 are believed to be involved in the regulation and maintenance of memory of the immune system. For immunochemists, however, Ab2 provide opportunities for new reagents for assay development. In certain areas, Ab2 have also been used to induce immune protection—in vaccine development. In the realm of fungal metabolites, Ab2 have been developed both as reagents for immunoassays.