Therapeutic antibody

A laboratory-produced or biologically derived antibody administered to prevent, diagnose, or treat disease by binding a specific molecule or cell.

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Antigen binding: The selective attachment of an antibody or other immune receptor to a molecular target. Binding a target is the shared first step behind an antibody’s therapeutic effects.
Immunoglobulin G: The most abundant antibody class in human blood, with four subclasses and a characteristic Y-shaped structure. Most established therapeutic antibodies use this class as their molecular scaffold.
Rituximab: A monoclonal antibody targeting CD20, used to treat certain B-cell cancers and autoimmune diseases. It exemplifies antibody-mediated depletion of a disease-associated cell population.
Small-molecule drug: A medicinal compound with low molecular mass that can often enter cells and bind intracellular targets. Small molecules can reach intracellular targets that conventional antibodies generally cannot.
Hybridoma technology: A method for producing monoclonal antibodies by fusing antibody-producing B cells with immortal myeloma cells. It established a reproducible route to monoclonal antibodies and enabled early therapeutic candidates.
Fc receptor: A cell-surface or soluble protein that binds the constant region of an antibody. Fc receptors let antibody-bound targets trigger immune-cell activity.
Monoclonal antibody: An antibody preparation whose molecules share one target specificity and derive from a single clone. Most therapeutic antibodies are designed as monoclonal products.
Trastuzumab: A monoclonal antibody targeting HER2, used in HER2-positive cancers. It demonstrates targeted treatment of tumors with high levels of a specific receptor.
Polyclonal antibody: A mixture of antibodies produced by different B-cell clones that recognize multiple epitopes. Unlike a monoclonal therapeutic, it contains a varied population of target-binding antibodies.
Humanization of antibodies: Engineering a nonhuman antibody to replace most of its sequence with human antibody components. Humanization reduced immune reactions that limited early therapeutic antibodies.