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Background
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Immunoglobulin G (IgG), is one of the most abundant proteins in human serum with normal levels between 8-17?mg/mL in ***** blood. IgG is important for our defence against microorganisms and the molecules are produced by B lymphocytes as a part of our adaptive immune response. The IgG molecule has two separate functions, to bind to the pathogen that elicited the response and to recruit other cells and molecules to destroy the antigen. The variability of the IgG pool is generated by somatic recombination and the number of specificities in an individual at a given time point is estimated to be 10e11 variants. Immunoglobulins, or antibodies, are a complex, heterogeneous mixture of proteins that exhibit two fundamental types of structural variation. Subtle structural differences in their antigen combining sites, or variable regions, account for their unique antigen binding specificities.Synonyms: Rat Immunoglobulin G1
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