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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.
One study has reported the isolation of a hybridoma cell line (clone 1E10), which produces a monoclonal antibody (IgM, k isotype). This monoclonal antibody shows specific immuno-cytochemical staining of nucleoli. [12] Tissues and tumours can be classified based on their expression of certain markers, with the help of monoclonal antibodies.
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.
This list of over 500 monoclonal antibodies includes approved and investigational drugs as well as drugs that have been withdrawn from market; consequently, the column Use does not necessarily indicate clinical usage.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.
By providing information on mechanism of action, epitope mapping is a critical component in therapeutic monoclonal antibody (mAb) development. Epitope mapping can reveal how a mAb exerts its functional effects - for instance, by blocking the binding of a ligand or by trapping a protein in a non-functional state.
It consists of two human monoclonal antibodies, casirivimab and imdevimab that must be mixed together and administered as an infusion or subcutaneous injection. [13] [8] [10] The combination of two antibodies is intended to prevent mutational escape. [14] It is also available as a co-formulated product. [13]
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The possibility of catalyzing a reaction by means of an antibody which binds the transition state was first suggested by William P. Jencks in 1969. [8] In 1994 Peter G. Schultz and Richard A. Lerner received the prestigious Wolf Prize in Chemistry for developing catalytic antibodies for many reactions and popularizing their study into a significant sub-field of enzymology.