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 whole molecule goat IgG. It also reacts with the light chains of other goat immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody may cross-react with immunoglobulins from other species.