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The immunoglobulin G (IgG) heavy chain is a component of the IgG antibody molecule, which is the most abundant class of immunoglobulins in serum. It consists of a variable domain (VH) for antigen binding and three constant domains (CH1, CH2, CH3) that mediate effector functions. The heavy chain defines the IgG subclass (IgG1, IgG2, IgG3, IgG4), each with distinct biological properties. IgG antibodies play a crucial role in adaptive immunity by neutralizing pathogens, activating complement, and recruiting immune cells.
Binding to target antigen, Fc-mediated effector functions (e.g., ADCC, CDC, phagocytosis), receptor blockade, signal modulation
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