Description
HP, as known as haptoglobin, is processed to yield both alpha and beta chains, which subsequently combine as a tetramer to produce haptoglobin. In blood plasma, haptoglobin binds free hemoglobin (Hb) released from erythrocytes with high affinity and thereby inhibits its oxidative activity. The haptoglobin-hemoglobin complex will then be removed by the reticuloendothelial system (mostly the spleen). Recombinant human HP protein, fused to His-tag at N-terminus, was expressed in E.coli