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Immunoglobulin G1 is the most abundant subclass of IgG in human serum, accounting for about 60% of IgG. It is a glycoprotein antibody (~146 kDa) formed by two heavy chains (gamma-1) and two light chains (either kappa or lambda), linked by disulfide bonds. Its structure enables high flexibility due to a long hinge region, allowing effective antigen binding and subsequent activation of immune effector mechanisms. IgG1 efficiently binds Fc gamma receptors and complements component C1q, contributing to potent immune defense through opsonization, complement activation, and antibody-dependent cellular cytotoxicity (ADCC). IgG1 is highly efficient in crossing the placenta, providing passive immunity to the fetus. Therapeutically, the IgG1 backbone is used to engineer monoclonal antibody drugs due to its favorable effector profile, but excessive activation or inappropriate immune targeting can result in adverse effects or autoimmune responses[1][3][4].
Antigen binding and neutralization via Fab region; Fc-mediated effector functions (ADCC: antibody-dependent cellular cytotoxicity; CDC: complement-dependent cytotoxicity); Immune complex formation and clearance
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