| 货号 | 700160-192Well |
| 描述 | Myeloperoxidase (MPO) is a member of the heme peroxidase superfamily and is stored within the azurophilic granules of leukocytes.1 MPO is found within circulating neutrophils, monocytes, and some tissue macrophages.2 A unique activity of MPO is its ability to use chloride as a cosubstrate with hydrogen peroxide to generate chlorinating oxidants such as hypochlorous acid, a potent antimicrobial agent.3 Recently, evidence has emerged that MPO-derived oxidants contribute to tissue damage and the initiation and propagation of acute and chronic vascular inflammatory diseases.4,5 The fact that circulating levels of MPO have been shown to predict risks for major adverse cardiac events and that levels of MPO-derived chlorinated compounds are specific biomarkers for disease progression, has attracted considerable interest in the development of therapeutically useful MPO inhibitors.6 MPO also oxidizes a variety of substrates, including phenols and anilines, via the classic peroxidation cycle. The relative concentrations of chloride and the reducing substrate determine whether MPO uses hydrogen peroxide for chlorination or peroxidation. Cayman’s MPO Peroxidation Fluorometric Assay provides a convenient fluorescence-based method for detecting the MPO peroxidase activity in both crude cell lysates and purified enzyme preparations. The assay utilizes the peroxidase component of MPO. The reaction between hydrogen peroxide and ADHP (10-acetyl-3,7-dihydroxyphenoxazine) produces the highly fluorescent compound resorufin. Resorufin fluorescence can be easily analyzed with an excitation wavelength of 530-540 nm and emission wavelength of 585-595 nm. The kit includes a MPO-specific inhibitor for distinguishing between MPO activity from MPO-independent fluorescence. |
| 别名 | MPO Peroxidation Assay Kit; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Yamada, M. and Kurahashi, K. Regulation of myeloperoxidase gene expression during differentiation of human myeloid leukemia HL-60 cells. The Journal of Biological Chemisty 259(5), 3021-3025 (1984). 2.Schultz, J. and Kaminker, K. Myeloperoxidase of the leucocyte of normal human blood.1 I. Content and localization. Archives of Biochemistry and Biophysics 96, 465-467 (1962). 3.Harrison, J.E. and Schultz, J. Studies on the chlorinating activity of myeloperoxidase. The Journal of Biological Chemisty 251(5), 1371-1374 (1976). 4.Podrez, E.A.,Abu-Soud, H.M. and Hazen, S.L. Myeloperoxidase-generated oxidants and atherosclerosis. Free Radical Biology & Medicine 28(12), 1717-1725 (2000). 5.Zhang, R.,Brennan, M.L.,Fu, X., et al. Association between myeloperoxidase levels and risk of coronary artery disease. Journal of the American Medical Association 286(17), 2136-2142 (2001). 6.Malle, E.,Furtmüller, P.G.,Sattler, W., et al. Myeloperoxidase: A target for new drug development? British Journal of Pharmacology 152, 838-854 (2007). | |
| 运输条件 | Wet ice in continental US; may vary elsewhere |
| 存放说明 | 4 |
| 稳定性 | ≥ 6 months |
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