Fragment antigen-binding

Fragment antigen-binding (also known as Fab) is a region on an antibody that binds to antigens. It is the most crucial part of the antibody, as it is responsible for the specific recognition and binding to the antigen. The Fab region is composed of one constant and one variable domain of each of the heavy and the light chain. These domains shape the antigen-binding site at the amino terminal end of the monomer.

Structure[edit | edit source]

The Fab fragment includes a complete light chain, and the VH and CH1 domains of the heavy chain. In other words, the Fab fragment is composed of four domains: VH, CH1, VL, and CL. The variable domains from the heavy and light chains pair to form the antigen-binding site at the amino terminal end of the monomer.

Function[edit | edit source]

The primary function of the Fab fragment is to bind to antigens. This is achieved through the variable domains of the heavy and light chains. These domains are responsible for recognizing and binding to the specific antigen. The constant domains of the light chain and the first domain of the heavy chain provide structural support.

Clinical Significance[edit | edit source]

The Fab fragment is of significant clinical importance. It is used in the development of monoclonal antibodies, which are used in the treatment of various diseases, including cancer, autoimmune diseases, and infectious diseases. The ability to produce monoclonal antibodies that only contain the Fab region allows for the specific targeting of disease cells without triggering an immune response.

See Also[edit | edit source]

Fragment antigen-binding Resources
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