Serum IgG autoantibodies consistently bind to diverse antigens in many human organs. A.

<p>Human liver, kidney, lung, and brain tissue lysates were separated by SDS-PAGE and then probed with human serum. As indicated by the many immunoreactive protein bands of differing molecular weights, serum IgG autoantibodies bind to a variety of common and organ-specific SDS-denatured antigens. <b>B</b>. In western blots, proteins from human brain extract were probed with human serum (HS-I and HS-II) as primary antibodies. Serum samples at three timepoints, T1, T2 and T3, were collected from the same individual (HS-I) over a period of four years. Serum samples T1’ and T2’ were collected from a different individual (HS-II) over a period of two years. Consistent patterns of serum IgG immunoreactivity were specific to individuals and appeared to remain stable over time.