* Antibodies, or immunoglobulins, are a family of structurally related glycoproteins produced in membrane-bound or secreted form by B lymphocytes.
* Membrane-bound antibodies serve as receptors that mediate the antigen-triggered activation of B cells.
* Secreted antibodies function as mediators of specific humoral immunity by engaging various effector mechanisms that serve to eliminate the bound antigens.
* The antigen-binding regions of antibody molecules are highly variable, and any one individual has the potential to produce more than 1011 different antibodies, each with distinct antigen specificity.
* All antibodies have a common symmetric core structure of two identical covalently linked heavy chains and two identical light chains, each linked to one of the heavy chains. Each chain consists of two or more independently folded Ig domains of about 110 amino acids containing conserved sequences and intrachain disulfide bonds.
* The N-terminal domains of heavy and light chains form the V regions of antibody molecules, which differ among antibodies of different specificities. The V regions of heavy and light chains each contain three separate hypervariable regions of about 10 amino acids that are spatially assembled to form the antigen-combining site of the antibody molecule.
* Antibodies are classified into different isotypes and subtypes on the basis of differences in the heavy chain C regions, which consist of three or four Ig C domains, and these classes and subclasses have different functional properties. The antibody classes are called IgM, IgD, IgG, IgE, and IgA. Both light chains of a single Ig molecule are of the same light chain isotype, either k or X, which differ in their single C domains.
* Most of the effector functions of antibodies are mediated by the C regions of the heavy chains, but these functions are triggered by binding of anti
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Therapeutic Applications of Antibodies
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