Immunoglobulin G (IgG) is a member of the immunoglobulin superfamily of glycoproteins that plays a central role in the adaptive immune response.1 It is produced by B cells and later secreted by plasma cells and is the most abundant circulating antibody in human and mouse serum.1,2,3 IgG consists of two heavy chains of approximately 50 kDa each and two light chains of approximately 25 kDa each.1 The heavy chains are linked together by disulfide bonds to form an Fc region and also combine with the light chains to form the Fab region, which mediate receptor and antigen binding, respectively.4 IgG is produced following IgM class-switching in response to infection and is involved in numerous humoral host defense responses, including antibody-dependent cell-mediated cytotoxicity (ADCC), toxin neutralization, and pathogen opsonization.2 IgG exists as four isotypes in mice: IgG1, IgG2b, IgG3, and, in a strain-specific manner, IgG2a or IgG2c.5,6 Formulations containing humanized, chimeric, or murine IgG monoclonal antibodies have been used in the treatment of inflammatory diseases, such as ulcerative colitis, rheumatoid arthritis, and asthma, as well as cancer.7 Cayman’s IgG Fc (mouse) Monoclonal Antibody (Clone RMG06) can be used for ELISA. The antibody recognizes the Fc region of IgG from mouse samples.WARNING This product is not for human or veterinary use.
