Antibodies, also called as immunoglobulin, is a protein produced by plasma cells in response to specific antigens. These antibodies can be used as therapeutic as well as diagnostic purposes for several indications, including cancers, autoimmune disorders, inflammatory & infectious diseases and others.
How antibodies work
When a foreign material enters the body, the immune system recognises it as foreign because the molecules on the antigen's surface differ from those found in the body. To destroy the intruder, the immune system employs a number of processes, one of which is the generation of antibodies. Antibodies are produced by B lymphocytes, which are specialised white blood cells (or B cells). When an antigen adheres to the B-cell surface, it stimulates the B cell to divide and mature into a clone, which is a group of identical cells. Millions of antibodies are secreted into the bloodstream and lymphatic system by mature B cells, known as plasma cells.
Antibodies structure and classes
Each antibody molecule is nearly identical to the antigen receptor of the B cell that generated it. These proteins have two pairs of polypeptide chains (lengths of amino acids connected by peptide bonds) that form a flexible Y shape. The Y's stem is made up of one end of two identical heavy chains, while each arm is made up of the remaining portion of a heavy chain plus a smaller protein known as the light chain. The two light chains are also the same. The consistent area refers to the fact that the stem and bottom of the arms of specific kinds of antibodies are quite identical.. The tips of the arms, however, are highly variable in sequence. It is these tips that bind antigen. Thus each antibodies has two identical antigen-binding sites, one at the end of each arm, and the antigen-binding sites vary greatly among antibodies.
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