Anti-HO-1 Antibody__Rabbit Anti-Human HO-1 Polyclonal PF-4840154
Storage Buffer
PBS pH 7.4, 50% glycerol, 0.09% sodium azide
Storage Temperature
-20ºC
Shipping Temperature
Blue Ice or 4ºC
Purification
Protein A purified
Clonality
Polyclonal
Specificity
Detects ~32kDa.
Cite This Product
Rabbit Anti-Human HO-1 Polyclonal (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPC-112)
Certificate of Analysis
1 µg/ml of SPC-112 was sufficient for detection of HO-1 in 10 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.
References PubMed ID::http://www.ncbi.nlm.nih.gov/pubmed/19129279
Alternative Names
Heme oxygenase 1 Antibody, Hemox Antibody, HMOX1 Antibody, HO1 Antibody, HO 1 Antibody, HSP32 Antibody
Research Areas
Cancer, Oxidative Stress
Cellular Localization
Endoplasmic Reticulum, Microsome
Accession Number
NP_002124.1
Gene ID
3162
Swiss Prot
P09601
Scientific 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).
References
1. Froh M. et al. (2007) World J. Gastroentereol 13(25): 3478-86.
2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47.
3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411–419.
4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8.
5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 10925–10930.
6. Yet S.F., et al. (2003) FASEB J. 17: 1759–1761.
7. Yachie A., et al. (1999) J Clin Invest. 103: 129–135.
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).
2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47.
3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411–419.
4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8.
5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 10925–10930.
6. Yet S.F., et al. (2003) FASEB J. 17: 1759–1761.
7. Yachie A., et al. (1999) J Clin Invest. 103: 129–135.