|Other Names||Heme oxygenase 1, HO-1, HMOX1, HO, HO1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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.|
|Cellular Location||Microsome. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side|
|Tissue Location||Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level)|
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Heme oxygenase, an essential enzyme in heme catabolism,cleaves heme to form biliverdin, which is subsequently converted tobilirubin by biliverdin reductase, and carbon monoxide, a putativeneurotransmitter. Heme oxygenase activity is induced by itssubstrate heme and by various nonheme substances. Heme oxygenaseoccurs as 2 isozymes, an inducible heme oxygenase-1 and aconstitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the hemeoxygenase family.
Wu, M.M., et al. Toxicol. Appl. Pharmacol. 248(3):226-233(2010)Bolisetty, S., et al. J. Am. Soc. Nephrol. 21(10):1702-1712(2010)Bao, W., et al. PLoS ONE 5 (8), E12371 (2010) :Wu, M.M., et al. J. Biomed. Sci. 17, 70 (2010) :Wang, X., et al. PLoS ONE 5 (8), E11934 (2010) :
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