Haptoglobin ELISA

Acute phase proteins are plasma proteins which increase in concentration following infection, inflammation or trauma. The first acute phase protein to be recognized was discovered in humans by Tillet and Frances in 1930 (1). Haptoglobin (Hp) is a heterogeneous plasma protein mostly synthesized by the liver. The haptoglobin monomer consists of two heavy chains, beta chains (40 kD) and two light chains, alpha chains, alpha 1 (9 kD) and alpha 2 (16 kD) that are linked disulfide bonds. The three major haptoglobin types are; Hp1-1 which is monomeric (98kD), Hp1-2 is polymeric at about 200 kD, and Hp2-2 at about 400 kD. The levels in serum rise quickly following acute tissue damage within 24 to 48 hours and also fall very rapidly once the stimulus is removed. In fact, haptoglobin levels are decreased in hemolytic anemia. Haptoglobin has a high affinity for hemoglobin (Hb) and its function appears to be to prevent loss of hemoglobin in urine which would lead to loss of iron. Investigations over the past few years have shown that quantification of haptoglobin in plasma or serum can provide valuable information in the research of disease not only in humans, but in companion animals and farm herds as well (2). =