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Overview of therapeutic monoclonal antibodies

John P Manis, MD
Section Editor
Daniel E Furst, MD
Deputy Editors
Jennifer S Tirnauer, MD
Anna M Feldweg, MD


Immunoglobulin molecules (antibodies) are multifunctional components of the immune system. Antibodies facilitate numerous cellular and humoral reactions to a variety of antigens, including those of the host (self) and foreign substances.

Most antibodies produced as part of the normal immune response are polyclonal, meaning that they are produced by a number of distinct B lymphocytes, and, as a result, they each have a slightly different specificity for the target antigen (eg, by binding different epitopes or binding the same epitope with different affinities). However, it is possible to produce large quantities of an antibody from a single B-cell clone.

Since 1985, approximately 100 independent monoclonal antibodies (mAbs) have been designated as drugs. Available mAbs are directed against a large number of antigens and used for the treatment of immunologic diseases, reversal of drug effects, and cancer therapy. The World Health Organization (WHO), which is responsible for therapeutic mAb nomenclature, reported in 2017 that over 500 mAb names have been provided. (See 'Naming convention for therapeutic mAbs' below.)

This topic will provide an overview of therapeutic mAbs, including their mechanisms of action, production, modifications, nomenclature, administration, and adverse effects.

Separate topic reviews discuss clinical uses of polyclonal antibodies, including subcutaneous, intramuscular, and intravenous immune globulin products (SCIG, IMIG, and IVIG, respectively):

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Literature review current through: Dec 2017. | This topic last updated: Dec 06, 2017.
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