Antibodies are the immune-related proteins that are produced by the humoral immune system consisting of B cells. They play a defensive role in the body against invading pathogens and other substances such as bacteria, viruses, etc. They bind to the invading foreign particles. They are also called immunoglobulins (Ig). These antibodies are very specific against heir antigens. It is known as “antibody specificity”.


These are Y-shaped molecules. They consist of two light chains (called L chains) and two heavy chains (called H chains) joined together and form this “Y” shaped molecule. The tip of the “Y” has an antigen-binding site where an antigen binds. The sequence of amino acids varies greatly on this tip of proteins among different antibodies.

It is a variable region of the antibody and may have a sequence of 110 to 130 amino acids. It gives specificity to the binding site. The variable region is composed of ends of both heavy and light chains. This region can be cleaved by treating the antibody with a protease. Antibodies can be classified into 5 major classes IgG, IgD, IgM, IgE, and IgA based on their function and constant region structure.

How many antibodies are produced?

The variable region of the heavy chain differs in antibodies produced by different B cells, but is the same for all antibodies produced by a single B cell or B cell clone. The variable region of each heavy chain is approximately 110 amino acids long and is composed of a single Ig domain.

How are primary antibodies produced?

MAbs are produced from a single B-cell clone of an animal and hence are directed against only one epitope of an antigen. PAbs are produced from multiple B-cell clones of an animal, and have a heterogeneous mix of antibodies that are directed against several epitopes of an antigen

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