Anti-Human IgG3 Magnetic Beads

Human IgG3 is one of the four subclasses of immunoglobulin G (IgG) antibodies. It has a unique structure characterized by an extended and flexible hinge region, which is much longer than the other IgG subclasses. This elongated hinge allows greater flexibility and movement of the Fab arms relative to the Fc region, contributing to IgG3's potent effector functions such as complement activation and binding to Fc receptors. However, IgG3 also has a shorter half-life compared to other IgG subclasses, primarily due to an arginine at position 435 that impairs its binding to the neonatal Fc receptor (FcRn) responsible for antibody recycling. Notably, IgG3 exhibits extensive allotypic diversity, with over 15 known allelic variations in the hinge region length and sequence. This structural variability influences IgG3's effector functions and has implications for its therapeutic potential. Protein function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins- secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). [The UniProt Consortium]