Hemopexin Human

Hemopexin (HPX) is a glycoprotein found in human blood plasma, known for its exceptional ability to bind heme with the highest affinity of any known protein . This binding capability is crucial for maintaining low toxicity levels in the blood and conserving valuable resources that would otherwise be lost through urination .

Hemopexin is composed of a single 60-kDa peptide chain and is primarily expressed in the liver . It plays a pivotal role in the immune defense against hemolytic stress by binding free heme released during the breakdown of red blood cells . This binding prevents heme from exerting its toxic effects and facilitates its safe transport to the liver for degradation and recycling .

Recombinant human hemopexin is produced using advanced biotechnological methods, typically involving the expression of the hemopexin gene in a suitable host cell line, such as mouse myeloma cells . The recombinant protein is then purified to achieve high purity levels, often exceeding 90% as determined by SDS-PAGE under reducing conditions . This recombinant form retains the heme-binding properties of the native protein and is used in various research and therapeutic applications .

Recombinant hemopexin has been studied for its potential therapeutic applications, particularly in conditions involving excessive free heme, such as hemolytic anemias and sepsis . It has been shown to inhibit the synergy of heme with lipopolysaccharides (LPS) on tumor necrosis factor (TNF) production from monocytes, thereby reducing inflammation . Additionally, recombinant hemopexin has been evaluated for its effects on neutrophil chemotaxis and protease activity, with findings suggesting that it does not directly affect chemotaxis but may decrease heme-driven chemotaxis and secondary inflammation .