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Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.
Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively. CDRs are where these molecules bind to their specific antigen and their structure/sequence determines the binding activity of the respective antibody.
This list of over 500 monoclonal antibodies includes approved and investigational drugs as well as drugs that have been withdrawn from market; consequently, the column Use does not necessarily indicate clinical usage. See the list of FDA-approved therapeutic monoclonal antibodies in the monoclonal antibody therapy page.
The scheme is useful when comparing these variable regions between antibodies. [1] Its foundations were laid by the American biomedical scientist Elvin A. Kabat, who started collecting and aligning amino acid sequences of human and mouse Bence Jones proteins and immunoglobulin light chains in 1969.
In immunology, antibodies (immunoglobulins (Ig)) are classified into several types called isotypes or classes. The variable (V) regions near the tip of the antibody can differ from molecule to molecule in countless ways, allowing it to specifically target an antigen (or more exactly, an epitope). In contrast, the constant (C) regions only occur ...
Antibody (or immunoglobulin) structure is made up of two heavy-chains and two light-chains.These chains are held together by disulfide bonds.The arrangement or processes that put together different parts of this antibody molecule play important role in antibody diversity and production of different subclasses or classes of antibodies.