Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed on purified antibody under both reducing and non-reducing conditions. Antibody was mixed with loading buffer and run in 10% polyacrylamide gel, with the thiol reagent 2-Mercaptoethanol added to the loading buffer for reducing conditions (to cleave the disulfide bonds between the polypeptides). Gels were stained with Coomassie blue for protein band detection of individual heavy and light chains of the antibody.