Anti-Human IgG1 Magnetic Beads

Human IgG1 is the most abundant subclass of IgG antibodies, representing 60-70% of total IgG in human serum. IgG1 has a flexible structure with a longer hinge region compared to other IgG subclasses, allowing for greater mobility of the Fab fragments relative to the Fc region. This flexibility affects IgG1's ability to bind and activate the classical complement pathway through C1q, as well as its binding to Fc receptors (FcgammaR) on phagocytic cells to mediate antibody-dependent cell-mediated cytotoxicity (ADCC) and phagocytosis. Deficiencies or abnormalities in IgG1 levels or function have been associated with various disease states. IgG1 deficiency is often linked to hypogammaglobulinemia, as IgG1 makes up the majority of total IgG, and low IgG1 levels can lead to increased susceptibility to viral infections. Conversely, excessive or dysregulated IgG1 responses have been implicated in autoimmune diseases and allergic disorders. 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]