Immunoglobulins are Y-shaped globular proteins that are about 10nm in size and 150kDa in molecular weight - Christine Leduc PharmD


image by: Medical Laboratory Scientist

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Immunoglobulins (Ig)

Though the general structure of all antibodies is very similar, that small region at the tip of the protein is extremely variable. This allows millions of antibodies with different tip structures to exist. Each of these variants can bind to a different antigen. This enormous diversity of antibodies allows the immune system to recognize an equally wide variety of antigens.

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 Immunoglobulins (Ig)

There are five main types of immunoglobulins, each immunoglobulin can have a different binding site that matches a specific antigen.


A group of “antibody” proteins which form the “humoral” immune system and are produced by B lymphocytes


Antibodies or immunoglobulins have two light chains and two heavy chains in a light-heavy-heavy-light structure arrangement. The heavy chains differ among classes. They have one Fc region that mediates biological functions (e.g., the binding capacity to cellular receptors) and a Fab region containing antigen-binding sites.

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