HO1 protein-GST fusion

Recombinant full-length human HO1 was expressed in E. coli cells using an N-Terminal Glutathione-S-Transferase fusion protein. The purity was determined to be >95% by densitometry. Protein function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. [The UniProt Consortium]