Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin， lung， and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury， and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system （generally the spleen）. As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body， haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin， haptoglobin sequesters the iron inside hemoglobin， preventing iron-utilizing bacteria from benefitting from hemolysis.
Haptoglobin consists of two ?- and two ?-chains， connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist （Hp 1-1， Hp 2-1， and Hp 2-2）. Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active， and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy， the incidence of coronary artery disease in type 1 diabetes， Crohn’s disease， inflammatory disease behavior， primary sclerosing cholangitis， susceptibility to idiopathic Parkinson’s disease， and a reduced incidence of Plasmodium falciparum malaria.
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人血浆中提取纯化
溶解建议
Sterile Filtered White lyophilized （freeze-dried） powder. Lyophilized from 0.02M NH4HCO3. May contain traces of buffer salts.
保存建议
Human Haptoglobin although stable at room temperature for 3 weeks， should be stored between 2-8℃.
