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.TRITC (tetraethyl rhodamine isothiocyanate) is the form of fluorescein used for conjugation to all of our antibodies and purified proteins, with the exception of streptavidin. This monoclonal antibody can be used to detect the light chain of goat immunoglobulin.