Rabbit anti-Mouse, Rat HO-1 (Rat) Polyclonal Antibody | anti-Hmox1 antibody

HO-1 (Rat) Antibody: PerCP

Cat. Num. AAA805430

• Gene Names: Hmox1; Ho1; Heox; Hmox; Ho-1; HEOXG; hsp32
• Reactivity: Mouse, Rat
• Applications: Western Blot
• Synonyms: HO-1 (Rat); Polyclonal Antibody; HO-1 (Rat) Antibody: PerCP; Heme oxygenase 1; Hemox; HMOX1; HO1; HO 1; Hsp32; anti-Hmox1 antibody

• Host: Rabbit
• Reactivity: Mouse, Rat
• Clonality: Polyclonal
• Form/Format: Protein A Purified
• Concentration: 1mg/ml (varies by lot)
• Sequence Length: 289

• Applicable Applications for anti-Hmox1 antibody: Western Blot (WB)
• Application Notes: 1:500-1000 for WB
• Conjugate: PerCP
• Storage Buffer: PBS pH 7.4, 0.09% azide, 50% glycerol.
• Preparation and Storage: -20 degree C

Related Product Information for anti-Hmox1 antibody

Background Info: Detects an ~32kDa protein, corresponding to the molecular mass of HO-1 on SDS Page Immunoblots. Does not cross-react with HO-2.

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).

Product Categories/Family for anti-Hmox1 antibody

Heat Shock; Oxidative Stress

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.
1. Bae, J.W., Kim, M.J., Jang, C.G. and Lee, S.Y. (2010). Protective effects of heme oxygenase-1 against MPP(+)-induced cytotoxicity in PC-12 cells. Neurol Sci. 31 (3), 307-313. doi: 10.1007/s10072-010-0216-6

NCBI and Uniprot Product Information

• NCBI GI #: 6981032
• NCBI GeneID: 24451
• NCBI Accession #: NP_036712.1
• NCBI GenBank Nucleotide #: NM_012580.2
• UniProt Accession #: P06762; Q5BK87
• Molecular Weight: 33,006 Da
• NCBI Official Full Name: heme oxygenase 1
• NCBI Official Synonym Full Names: heme oxygenase (decycling) 1
• NCBI Official Symbol: Hmox1
• NCBI Official Synonym Symbols: Ho1; Heox; Hmox; Ho-1; HEOXG; hsp32
• NCBI Protein Information: heme oxygenase 1; heme oxygenase (decyclizing) 1
• UniProt Protein Name: Heme oxygenase 1
• UniProt Gene Name: Hmox1
• UniProt Synonym Gene Names: HO-1
• UniProt Entry Name: HMOX1_RAT

NCBI Description

catalyzes the oxidative cleavage of heme to biliverdin [RGD, Feb 2006]

Uniprot Description

HMOX1: 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 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family.

Protein type: Oxidoreductase; EC 1.14.99.3; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll

Cellular Component: endoplasmic reticulum membrane; perinuclear region of cytoplasm; endoplasmic reticulum; nucleolus; plasma membrane; caveola; cytosol; nucleus

Molecular Function: signal transducer activity; protein binding; enzyme binding; protein homodimerization activity; metal ion binding; phospholipase D activity; heme binding; oxidoreductase activity; heme oxygenase (decyclizing) activity

Biological Process: cell death; response to nicotine; negative regulation of smooth muscle cell proliferation; negative regulation of mast cell degranulation; positive regulation of smooth muscle cell proliferation; heme metabolic process; negative regulation of cell proliferation; erythrocyte homeostasis; regulation of transcription factor activity; heme catabolic process; small GTPase mediated signal transduction; regulation of blood pressure; phospholipid metabolic process; negative regulation of mast cell cytokine production; angiogenesis; negative regulation of neuron apoptosis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; healing during inflammatory response; protein homooligomerization; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of transcription factor activity; heme oxidation; cellular response to nutrient; negative regulation of DNA binding; iron ion homeostasis; positive regulation of angiogenesis; response to hydrogen peroxide; DNA damage response, signal transduction resulting in induction of apoptosis; response to estrogen stimulus; response to hypoxia; response to oxidative stress