Monoclonal antibody (mAb)

Monoclonal antibodies are laboratory-engineered immunoglobulins designed to recognize and bind specifically to a single antigen. They are produced by a single clone of B cells, making them highly specific for their intended target. Therapeutic monoclonal antibodies can be used to neutralize pathogens, block pathological signaling pathways, modulate or enhance the human immune response, deliver cytotoxic payloads directly to diseased cells, and assist in diagnostic applications. Humanized or fully human monoclonal antibodies help minimize immune reactions and are prevalent in modern therapeutics. Individual monoclonal antibodies are named according to their target; for example, trastuzumab targets HER2, rituximab targets CD20, and adalimumab targets TNF-alpha. The entry "Monoclonal antibodies" is not a therapeutic target itself but a modality—an approach for targeting. Each monoclonal antibody is specific for a therapeutic target (such as HER2, EGFR, PD-1), and so is not directly a single molecular entity, receptor, or enzyme. Therefore, it is considered "incorrect" when entered as a single target. For data structuring, individual monoclonal antibodies should be mapped to their specific target (e.g., HER2 receptor, CD20 antigen, PD-1 checkpoint) for proper classification and data enrichment.

Other names

Monoclonal immunoglobulinmAbtherapeutic antibodyhumanized antibodychimeric antibody

Binding and neutralization of target antigens; Blocking receptor-ligand interactions; Induction of immune effector functions (ADCC, CDC); Delivery of cytotoxic payloads (antibody-drug conjugates, radioisotopes); Inhibition of immune checkpoints.