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A general representation of the method used to produce monoclonal antibodies [1] [2] A monoclonal antibody (mAb, more rarely called moAb) is an antibody produced from a cell lineage made by cloning a unique white blood cell. All subsequent antibodies derived this way trace back to a unique parent cell.
In contrast to polyclonal antibodies, which are mixtures of many different antibody molecules, the monoclonal antibodies produced by each hybridoma line are all chemically identical. The production of monoclonal antibodies was invented by César Milstein and Georges J. F. Köhler in 1975.
Antibody-directed enzyme prodrug therapy (ADEPT) involves the application of cancer-associated monoclonal antibodies that are linked to a drug-activating enzyme. Systemic administration of a non-toxic agent results in the antibody's conversion to a toxic drug, resulting in a cytotoxic effect that can be targeted at malignant cells.
Humanized antibodies are antibodies from non-human species whose protein sequences have been modified to increase their similarity to antibody variants produced naturally in humans. [ 1 ] [ 2 ] The process of "humanization" is usually applied to monoclonal antibodies developed for administration to humans (for example, antibodies developed as ...
The principle of monoclonal antibody production, called hybridoma technology, was published in 1975 by Georges Köhler and César Milstein, [30] who were awarded the 1984 Medicine Nobel Prize for their discovery together with Niels Kaj Jerne. [31] Muromonab-CD3 was the first monoclonal antibody to be approved for clinical use in humans, in 1986 ...
The fragment antigen-binding region (Fab region) is a region on an antibody that binds to antigens. It is composed of one constant and one variable domain of each of the heavy and the light chain . The variable domain contains the paratope (the antigen-binding site), comprising a set of complementarity-determining regions , at the amino ...
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