Haptoglobin is a glycoprotein composed of two alpha and two beta chains, forming a tetramer. The recombinant human haptoglobin (19-347 a.a) refers to a specific segment of the haptoglobin protein, spanning amino acids 19 to 347. This recombinant form is typically expressed in Escherichia coli (E. coli) and is often fused to a His-tag at the N-terminus to facilitate purification .
The primary function of haptoglobin is to bind free hemoglobin released during hemolysis. This binding prevents the loss of iron through the kidneys and protects the kidneys from damage by free hemoglobin. The haptoglobin-hemoglobin complex is then removed by the reticuloendothelial system, primarily in the liver and spleen.
Haptoglobin levels are measured in clinical settings to assess hemolytic anemia. Low levels of haptoglobin in the blood can indicate increased red blood cell destruction. Additionally, haptoglobin is an acute-phase protein, meaning its levels can increase in response to inflammation, infection, or trauma.
The recombinant form of haptoglobin (19-347 a.a) is produced using genetic engineering techniques. The gene encoding the desired segment of haptoglobin is inserted into an expression vector, which is then introduced into E. coli cells. These cells are cultured, and the recombinant protein is expressed and subsequently purified using chromatographic techniques .
Recombinant haptoglobin is used in various research applications, including studies on hemolysis, inflammation, and the acute-phase response. It is also utilized in the development of diagnostic assays and therapeutic interventions.
In summary, recombinant human haptoglobin (19-347 a.a) is a valuable tool in both research and clinical settings. Its ability to bind free hemoglobin and its role in the acute-phase response make it an important protein for studying and managing various medical conditions.