IgG, which is a type of antibody, is used as a drug substance for antibody drugs. It is known that IgG may form dimer, trimer, and aggregates due to mechanical stress in each process during manufacturing and environmental factors during transportation and storage. Since aggregates in antibody drugs can reduce drug efficacy and cause side effects, it is necessary to evaluate monomer, multimers, and aggregates for quality control. In 2014, the U.S. Food and Drug Administration (FDA) has provided guidance on the evaluation of immunogenicity of therapeutic protein products and recommended that the validity of each analysis result should be judged while comparing the results using multiple methods (Orthogonal Method) with different measurement principles for protein aggregates contained in biopharmaceuticals. This time, we show the results of measuring human serum-derived IgG reagent by size exclusion chromatography (SEC), which is one of the analytical methods for aggregates, and separating and detecting monomer, multimers, and aggregates.ResultsFigure 1 shows a UV chromatogram of a protein standard sample. As reference data, an RI chromatogram is also shown, which was measured by connecting an RI detector (RI-4030) downstream of the UV detector.