Anti-Human IgG antibody

Target data

Constant region of immunoglobulin (Ig) heavy chains. Igs are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound Igs serve as receptors, which upon binding to a specific antigen trigger the clonal expansion and differentiation of B lymphocytes into Ig-secreting plasma cells. Secreted Igs known as antibodies mediate the effector phase of humoral immunity by blocking the interaction of infectious antigens with cellular receptors (via the antigen-binding region) and eliciting effector mechanisms that lead to pathogen neutralization (via the constant region) (PubMed : 17576170, PubMed : 20176268, PubMed : 22158414). The antigen-binding region is formed by the variable domain of one heavy chain paired with the variable domain of its associated light chain. Each Ig molecule has two antigen-binding sites with remarkable affinity for a particular antigen due to V-(D)-J rearrangement, somatic hypermutations and affinity maturation of the variable domains upon antigen exposure (PubMed : 17576170, PubMed : 20176268, PubMed : 22158414). The constant region defines the Ig isotype that perform distinct sets of effector functions. B cells diversify and rearrange their Ig constant regions through class-switch recombination, a process by which the constant region is switched from one Ig isotype to another, namely from IgM and IgD to IgG, IgA and IgE (PubMed : 17576170, PubMed : 20176268, PubMed : 22158414). The constant region of Ig gamma-1 (IgG1) isotype interacts (via the fragment crystallizable, Fc) with receptors on innate immune cells and the complement system to mediate humoral effector functions, including antibody-dependent cellular cytotoxicity or phagocytosis, complement-dependent cytotoxicity and inflammatory responses.