Recent evidence validates a forgotten 40-year-old hypothesis: the MHC-related Fc receptor for IgG (FcRn) protects albumin from intracellular catabolic degradation, as it does for IgG, accounting for the uniquely long half-lives of both molecules and explaining their direct concentration-catabolism relationships. Albumin and IgG bind to FcRn at low pH but not at physiological pH. These two ligands bind independently of one another by distinctive mechanisms and to different surfaces of the receptor. Kinetic studies of FcRn-deficient mice indicate that, at steady-state, FcRn salvages from the degradative pathway a similar amount of albumin as is produced by mice and almost four-times more IgG than is produced. Thirty-fivefold more albumin than IgG molecules are protected from degradation by FcRn per unit time. It can be inferred that FcRn is expressed in nearly all cells. This receptor, originally described as transporting IgG from the mother to the fetus or neonate, now has a wider role central to the homeostatic regulation and conservation of both albumin and IgG throughout life.