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HO-2 polyclonal antibody

 
ADI-OSA-200-D 50 µg 269.00 USD
 
ADI-OSA-200-F 200 µg 541.00 USD
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Product Details

Alternative Name:HMOX2, Hsp32, Heat shock protein 32, Heme oxygenase 2
 
Host:Rabbit
 
Immunogen:Native rat HO-2 protein, isolated from rat testes.
 
UniProt ID:P23711
 
GenBank ID:J05405
 
Source:Purified from rabbit serum.
 
Species reactivity:Human, Mouse, Rat
Bovine, Crawfish, Dog, Guinea pig, Hamster, Monkey, Porcine, Rabbit, Sheep
 
Applications:ICC, IHC, IP, WB
 
Recommended Dilutions/Conditions:Western Blot (1:500, ECL)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Application Notes:Detects a band of ~36kDa by Western blot.
 
Purity Detail:Protein A affinity purified.
 
Formulation:Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
 
Shipping:Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background:Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; biliverdin and its product bilirubin are potent antioxidants; "free" iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferring receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'- UTRs of the mRNAs. To date, three identified heme oxygenase isoforms are part of the HO system that catalyze heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in heme degradation and HO activity decreases the levels of heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.
 
Regulatory Status:RUO - Research Use Only
 
HO-2 polyclonal antibody Immunohistochemistry
Immunohistochemistry analysis of frozen human prostate section stained using HO-2 pAb.
HO-2 polyclonal antibody Immunohistochemistry
Immunohistochemistry analysis of frozen mouse spinal cord section (stressed) stained using HO-2 pAb.
HO-2 polyclonal antibody Western blot
Western blot analysis of HO-2: Lane 1: MWM, Lane 2: HO-2 (human), (recombinant) (Prod. No.ADI-SPP-550), Lane 3: HeLa (Heat Shocked) Cell Lysate, Lane 4: L929 Cell Lysate, Lane 5: RK-13 Cell Lysate, Lane 6: CHO-K1 Cell Lysate
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HO-2 polyclonal antibody Immunohistochemistry HO-2 polyclonal antibody Immunohistochemistry HO-2 polyclonal antibody Western blot

Product Literature References

Heme Oxygenase 1 in Schwann Cells Regulates Peripheral Nerve Degeneration Against Oxidative Stress: M. Kim, et al.; ASN Neuro. 11, 1.7590914198389E+15 (2019), Abstract; Full Text
Loss of heme oxygenase-1 accelerates mesodermal gene expressions during embryoid body development from mouse embryonic stem cells: Y.L. Lai, et al.; Redox Biol. 15, 51 (2018), Abstract; Full Text
The protective mechanism of docosahexaenoic acid in mouse model of Parkinson: The role of heme oxygenase: A. Ozkan, et al.; Neurochem. Int. 101, 110 (2016), Application(s): Western blot analysis, mouse SN tissues, Abstract;
Heme oxygenase-1 ameliorates kidney ischemia-reperfusion injury in mice through extracellular signal-regulated kinase 1/2-enhanced tubular epithelium proliferation: H. Chen, et al. ; Biochim. Biophys. Acta 1852, 2195 (2015), Application(s): Western blot , Abstract;
Inhibition of dipeptidyl peptidase IV protects tacrolimus-induced kidney injury: S. Lim, et al.; Lab. Invest. 95, 1174 (2015), Application(s): Immunoblot analysis, Abstract;
Nerve growth factor induces anti-apoptotic heme oxygenase-1 in rat pheochromocytoma PC12 cells: K.D. Bloch, et al. ; J. Neurochem. 86, 1553 (2003), Application(s): WB using rat samples, Abstract;
Resistance to hyperoxia with heme oxygenase-1 disruption: role of iron: G. Yang, et al. ; Free Radic. Biol. Med. 34, 124 (2003), Application(s): WB using mouse samples, Abstract;
Differential effect of heme oxygenase-1 in endothelial and smooth muscle cell cycle progression: N.G. Abraham, et al. ; Biochem. Biophys. Res. Commun. 296, 1077 (2002), Application(s): WB using human samples, Abstract;
Regulation of cyclooxygenase by the heme-heme oxygenase system in microvessel endothelial cells: N.G. Abraham, et al. ; J. Pharmacol. Exp. Ther. 300, 188 (2002), Application(s): WB using rabbit samples, Abstract;
Altered expression of heme oxygenase-1 in the livers of patients with portal hypertensive diseases: Y. Ishimura, et al. ; Hepatology 33, 32 (2001), Application(s): IHC using human samples, Abstract;
Amyloid precursor proteins inhibit heme oxygenase activity and augment neurotoxicity in Alzheimer's disease: S.H. Snyder, et al. ; Neuron 28, 461 (2000), Application(s): IP using human & rat samples, Abstract;
Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system: evidence from genomic deletion of biosynthetic enzymes: J.H. Szurszewski, et al. ; PNAS 97, 1851 (2000), Application(s): IHC using mouse samples, Abstract;
Heme oxygenase 2 is present in interstitial cell networks of the mouse small intestine: J.H. Szurszewski, et al. ; Gastroenterology 114, 239 (1998), Application(s): IHC using mouse samples, Abstract;

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