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 Class switching to the IgG2b isotype occurs via TGF-β stimulation during the early immune response.7 IgG2b binds to activating Fcγ receptors (FcγRs) and is involved in complement fixation.5 Cayman’s IgG2b (mouse) Rabbit Monoclonal Antibody (Clone RM108) can be used for ELISA, flow cytometry (FC), immunoprecipitation (IP), and Western blot (WB) applications. The antibody recognizes the Fc region of non-reduced and reduced IgG2b at approximately 150 and 50 kDa, respectively, from mouse samples.WARNING This product is not for human or veterinary use.
