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The precipitin reaction provided the first quantitative assay for antibody. The precipitin reaction is based upon the interaction of antigen with antibody leading to the production of antigen-antibody complexes. To produce a precipitin reaction, varying amounts of soluble antigen are added to a fixed amount of serum containing antibody.
As more antigen is added, the amount of protein precipitated increases until the antigen/antibody molecules are at an optimal ratio. This is known as the zone of equivalence or equivalence point. When the amount of antigen in solution exceeds the amount of antibody, the amount of precipitation will decrease. This is known as the antigen excess ...
The antibody that fails to react is known as the blocking antibody and prevents the precipitating antibody from binding to the antigens. Thus the proper precipitation reaction does not take place. However, when the serum is diluted, the blocking antibody is as well and its concentration decreases enough for the proper precipitation reaction to ...
Immunoprecipitation of intact protein complexes (i.e. antigen along with any proteins or ligands that are bound to it) is known as co-immunoprecipitation (Co-IP). Co-IP works by selecting an antibody that targets a known protein that is believed to be a member of a larger complex of proteins.
Immunodiffusion is a laboratory technique used to detect and quantify antigens and antibodies by observing their interactions within a gel medium. [1] This technique involves the diffusion of antigens and antibodies through a gel, usually agar, resulting in the formation of a visible precipitate when they interact.
[1] [2] [5] The antigen is quantitated by measuring the diameter of the precipitin circle and comparing it with the diameters of precipitin circles formed by known quantities or concentrations of the antigen. [1] [2] [3] [6] Antigen-antibody complexes are small and soluble when in antigen excess. Therefore, precipitation near the center of the ...
An immune complex, sometimes called an antigen-antibody complex or antigen-bound antibody, is a molecule formed from the binding of multiple antigens to antibodies. [1] The bound antigen and antibody act as a unitary object, effectively an antigen of its own with a specific epitope .
He and his collaborators Forrest E. Kendall (1899–1987) [7] and Elvin A. Kabat formulated a quantitative theory of precipitin and other immune reactions, which showed that such reactions unfolded in three distinct stages and which posited that antigens and antibodies were bi-or multivalent, meaning that they could combine in varying proportions.