HO-1 ELISA Kit

Heme-oxygenase is a ubiquitous enzyme that catalyzes the initial and rate-limiting steps in heme catabolism yielding equimolar amounts of biliverdin, iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin and the free iron is sequestered to ferritin. These products have important physiological effects as carbon monoxide is a potent vasodilator; biliverdin and bilirubin are potent antioxidants; and the free iron increases oxidative stress and regulates the expression of many mRNAs. There are three isoforms of heme-oxygenase, HO-1, HO-2 and HO-3; however HO-1 and HO-2 are the major isoforms as they both have been identified in mammals. HO-1, also known as heat shock protein 32, is an inducible isoform activated by most oxidative stress inducers, cytokines, inflammatory agents and heat shock. HO-2 is a constitutive isoform which is expressed under homeostatic conditions. HO-1 is also considered to be a cytoprotective factor in that free heme is highly reactive and cytotoxic, and secondly, carbon monoxide is a mediator inhibiting the inflammatory process and bilirubin is a scavenger for reactive oxygen, both of which are the end products of heme catalyzation. It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency, susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation. Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress.

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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.