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Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective.Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc portion of rat IgG heavy chain but not with the Fab portion of rat IgG. No antibody was detected against rat IgM or non-immunoglobulin serum proteins. The antibody exhibits inherent minimal cross-reaction to mouse serum proteins and has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine, horse and mouse serum proteins. The antibody may cross-react with immunoglobulins from other species.