In our experience, some examples of mouse monoclonal antibodies of anti-B blood group specificity develop a precipitate when stored at 4 degrees C. This poses problems during the preparation of blood grouping reagents containing anti-B, and in the storage and use of such reagents. Here we show that this problem can be circumvented by alteration of the glycan moiety of the secreted immunoglobulin, either by glycosidase treatment of the partially purified immunoglobulin, or by the addition of glycan processing inhibitors to the hybridoma cell cultures. These findings have importance for the manufacture of monoclonal antibodies, and highlight a possible new role for carbohydrate in immunoglobulin interaction and immune complex formation.