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Heme Oxygenase (Decycling) 1 (HMOX1) antibody

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Dog (Canine), Human, Mouse (Murine), Rat (Rattus)
(251), (159), (138), (46), (30), (28), (26), (24), (23), (19), (3), (2), (2), (2)
(232), (90), (2), (1)
(22), (20), (11), (10), (9), (9), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7)
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blotting (WB)
(293), (141), (119), (83), (72), (50), (39), (25), (14), (5), (3), (1), (1), (1)
Pubmed 7 references available
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Quantity 25 μg
Shipping to United States ( )
Availability Will be delivered in 3 to 4 Business Days
Immunogen Human heme-oxygenase (HO-1) synthetic multiple antigenic peptide
Specificity Detects ~32 kDa.
Purification Protein A Purified
Alternative Name HO-1 (HMOX1 Antibody Abstract)
Background 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 (1). 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 (2). 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 (3). 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 (4). It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency (5), susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation (7). Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress (4).
Cellular Localization: Endoplasmic Reticulum | Microsome
Gene ID 3162
NCBI Accession NP_002124
UniProt P09601
Application Notes Recommended Dilution: WB (1:1000), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Background publications Froh, Conzelmann, Walbrun et al.: "Heme oxygenase-1 overexpression increases liver injury after bile duct ligation in rats." in: World journal of gastroenterology : WJG, Vol. 13, Issue 25, pp. 3478-86, 2007 (PubMed).

Brydun, Watari, Yamamoto et al.: "Reduced expression of heme oxygenase-1 in patients with coronary atherosclerosis." in: Hypertension research : official journal of the Japanese Society of Hypertension, Vol. 30, Issue 4, pp. 341-8, 2007 (PubMed).

Yet, Layne, Liu et al.: "Absence of heme oxygenase-1 exacerbates atherosclerotic lesion formation and vascular remodeling." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 17, Issue 12, pp. 1759-61, 2003 (PubMed).

Elbirt, Bonkovsky: "Heme oxygenase: recent advances in understanding its regulation and role." in: Proceedings of the Association of American Physicians, Vol. 111, Issue 5, pp. 438-47, 1999 (PubMed).

Yachie, Niida, Wada et al.: "Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency." in: The Journal of clinical investigation, Vol. 103, Issue 1, pp. 129-35, 1999 (PubMed).

Poss, Tonegawa: "Reduced stress defense in heme oxygenase 1-deficient cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 20, pp. 10925-30, 1997 (PubMed).

Maines, Trakshel, Kutty: "Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible." in: The Journal of biological chemistry, Vol. 261, Issue 1, pp. 411-9, 1986 (PubMed).

Catalog No. ABIN361673
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