Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by the immune system in response to the presence of foreign substances called antigens. These antigens can be from pathogens such as bacteria, viruses, and other microorganisms, as well as from non-living substances like toxins and chemicals.
Antibodies are composed of four polypeptide chains - two identical heavy chains and two identical light chains. Each chain contains constant and variable regions. The variable regions are crucial for the specificity of antibody-antigen binding, as they contain the antigen-binding site. The constant regions determine the antibody's class and function.
Antibodies function by recognizing and binding to specific antigens, marking them for destruction by other immune cells. This process can lead to the neutralization of pathogens, the activation of the complement system, or the tagging of antigens for phagocytosis.
There are five main classes of antibodies: IgG, IgM, IgA, IgD, and IgE. Each class has distinct functions and distribution within the body. IgG, for example, is the most abundant antibody, found in blood and tissue fluids, and provides long-term immunity. On the other hand, IgE is involved in allergic reactions and defense against parasitic infections.
Understanding antibodies is crucial in comprehending the immune response and various aspects of immunology. It also has implications in medical research, diagnostics, and healthcare.
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