Haptoglobin (Hp) is a blood plasma protein that functions to bind free Hemoglobin that has been released from erythrocytes, thereby inhibiting its oxidative activity. During this process, Haptoglobin sequesters the iron within Hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis. This function suggests that Haptoglobin concentrations may increase in response to inflammation. The resulting Haptoglobin-Hemoglobin complex is then removed by the reticulo-endothelial system. Due to cleavage of a common precursor protein during protein synthesis, Haptoglobin consists of two α and two β chains, connected by disulfide bridges. In human, Haptoglobin exists in two allelic forms designated Haptoglogin 1 (Hp1) and Haptoglobin 2 (Hp2), where Hp2 is the result of a partial Hp1 gene duplication. There are three known phenotypes of human Haptoglobin: Hp1-1, Hp2-1 and Hp2-2, which may be associated with diabetes and cardiovascular disease pathology and a susceptibility to Parkinson's and Crohn's disease. Haptoglobin levels are useful in diagnosing hemolytic anemia, the abnormal breakdown of red blood cells. Haptoglobin is expressed in mammalian hepatocytes as well as other tissues such as skin, lung and kidney.