- CITATIONS: 1
|Application ||WB, FC, E|
|Calculated MW||32819 Da|
|Antigen Region||177-204 aa|
|Other Names||Heme oxygenase 1, HO-1, HMOX1, HO, HO1|
|Target/Specificity||This HMOX1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 177-204 amino acids from the Central region of human HMOX1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HMOX1 Antibody (Center) is for research use only and 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)|
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 to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase 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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