Representing approximately 75% of serum antibodies, IgG is the most common type of antibody found in the circulation. IgG molecules are created and released by plasma B cells. IgG antibodies are large molecules of about 150 kDa made of four peptide chains. It contains two identical class gamma heavy chains of about 50 kDa and two identical light chains of about 25 kDa. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves, which together form the Y-like shape. Each end of the fork contains an identical antigen binding site. The Fc regions of IgGs bear a highly conserved N-glycosylation site. There are four IgG subclasses (IgG1, 2, 3, and 4) in humans, named in order of their abundance in serum (IgG1 being the most abundant).
|Target Name:||Human IgG|
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