Antibodies, also known as immunoglobulins, are 150 kDa, Y-shaped proteins that are both a natural part of the immune system and a tool that can be used for a variety of research applications. Within the immune system, antibodies are produced by B cells.
To know more about antibodies, you can also navigate https://www.bosterbio.com/featured-products. They bind to proteins on the surface of extracellular pathogens such as parasites or microbes or proteins expressed on the surface of cells infected with microbes to trigger an immune cascade that clears these infections.
Anything that creates an antibody response in the immune system is called an antigen. The ability of antibodies to bind to proteins is also useful for research applications as it allows scientists to target specific proteins of interest.
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Once a protein is targeted to an antibody, you can visualize the protein using fluorescence or chemiluminescence, precipitate the protein from solution, or isolate the cells expressing that protein. Read on to learn more about antibodies and how they are used in the laboratory!
Antibodies have two regions: Fab or antigen-binding region and Fc or crystallization region. Each antibody molecule consists of two immunoglobulins (Ig) heavy chains and two Ig light chains.
The Fc region and part of the Fab region consist of an Ig heavy chain and the other Fab region is supplemented by an Ig light chain. The variable regions of the heavy and light chains determine which antigens the antibody recognizes and binds to.