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Western blot analysis of Heme Oxygenase 1 on SW13 lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of Heme Oxygenase 1.
HeLa
BD Transduction Laboratories™ Purified Mouse Anti-Heme Oxygenase 1
BD Transduction Laboratories™ Purified Mouse Anti-Heme Oxygenase 1
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
The 23/Heme Oxygenase 1 monoclonal antibody specifically recognizes Heme oxygenase 1 (HO-1), also known as Heat Shock Protein 32 (HSP32). HO-1 is a 32 kDa monooxygenase encoded by HMOX1. Heme oxygenases 1 and 2 (HO-1, HO-2) cleave the heme molecule, resulting in the production of carbon monoxide (CO) and biliverdin. While HO-2 is constitutively expressed in tissues, HO-1 is rapidly induced by several stimuli such as lutathione depletion, hemin, heat shock, heavy metals, oxidative stress, oxidized LDL, anoxia, and endotoxic shock. HO-1 and its byproducts have potent antioxidant, antiproliferative, anti-inflammatory and anti-apoptotic effects in various cell types. In humans, HO-1 deficiency is associated with susceptibility to oxidative stress, increased inflammation and endothelial cell damage. In immune cells, HO-1 is required for the activation of interferon (IFN) regulatory factor 3 (IRF3) after Toll-like receptor 3 or 4 stimulation or viral infection. It is also upregulated on T cells upon TCR stimulation.
Development References (4)
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Foresti R, Clark JE, Green CJ, Motterlini R. Thiol compounds interact with nitric oxide in regulating heme oxygenase-1 induction in endothelial cells. Involvement of superoxide and peroxynitrite anions. J Biol Chem. 1997; 272(29):18411-18417. (Biology). View Reference
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Ishikawa K, Navab M, Leitinger N, Fogelman AM, Lusis AJ. Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL. J Clin Invest. 1997; 100(5):1209-1216. (Biology). View Reference
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Suzuki M, Ishizaka N, Tsukamoto K. Pressurization facilitates adenovirus-mediated gene transfer into vein graft. FEBS Lett. 2000; 470(3):370-374. (Clone-specific: Western blot). View Reference
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Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S. Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem. 1988; 171(3):457-461. (Biology). View Reference
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