Recombinant Human HO1 Protein (Trx Tag)

Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HO-1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. HO-1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. HO-1 is involved in the regulation of cardiovascular function and response to a variety of stressors. Defects in HO-1 are the cause of Heme Oxygenase 1 deficiency, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues.

HSP; heme oxygenase; heme oxygenase (decycling) ; bK286B; HO-1 HMOX; HMOX1; HMOX1D; HO-1; HSP32; bK286B10;32 kD; D8Wsu38e; heat shock protein 32 kD; heat shock protein 32kD; Hemox; Hmox; HMOX 1; HO 1; HO-1 HMOX1; heme oxygenase (decycling) 1; heme oxygenase 1; heat shock protein;32-kD; HO; HO1; bK286B10; heme oxygenase 1; HMOX1D; HO-1; HSP32

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.