|Other Names||Heme oxygenase 2, HO-2, HMOX2, HO2|
|Format||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.|
|Cellular Location||Microsome. Endoplasmic reticulum.|
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Provided below are standard protocols that you may find useful for product applications.
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. Alternative splice variants encoding the sameprotein have been identified at this locus.
Abdel Aziz, M.T., et al. Andrologia 42(4):236-241(2010)Wang, Y., et al. J. Hum. Genet. 55(8):490-494(2010)He, J.Z., et al. J. Biol. Chem. 285(13):9452-9461(2010)Zhong, J.L., et al. Free Radic. Biol. Med. 48(2):196-206(2010)Yun, L., et al. Clin. Exp. Hypertens. 31(7):534-543(2009)
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