Myeloperoxidase Inhibitor Screening Assay Kit | Cayman Chemical
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Myeloperoxidase Inhibitor Screening Assay Kit

Item № 700170
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     2 x 96 wells $219.00 0.00

Pricing updated 2018-12-19. Prices are subject to change without notice.

  • Screen for inhibitors of MPO
  • Includes reagents to measure both the chlorination and peroxidation activities
  • Assay 45 samples in duplicate
  • Plate-based fluorometric measurement (ex 480-495 nm, em 515-525 nm, ex 530-540 nm, em 585-595 nm)
  • MPO Inhibitor Screening Assay Kit

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. Assays based on measurement of chlorination activity are more specific for MPO than those based on peroxidase substrates because peroxidases generally do not produce hypochlorous acid. However, it is important that when screening for MPO inhibition that both the chlorination and peroxidation activities be tested. This determines whether the inhibitor specifically interferes with the chlorination and/or peroxidation cycle or whether the inhibitor simply acts as a scavenger for hypochlorous acid. Also, many reversible inhibitors act by diverting MPO from the chlorinating cycle to the peroxidase cycle. Cayman’s MPO Inhibitor Screening Assay provides convenient fluorescence-based methods for screening inhibitors to both the chlorination and peroxidation activities of MPO. The chlorination assay utilizes the non-fluorescent 2-[6-(4-aminophenoxy)-3-oxo-3H-xanthen-9-yl]-benzoic acid (APF), which is selectively cleaved by hypochlorite (-OCl) to yield the highly fluorescent compound fluorescein.7 Fluorescein fluorescence is analyzed with an excitation wavelength of 480-495 nm and an emission wavelength of 515-525 nm. The peroxidation 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 is analyzed with an excitation wavelength of 530-540 nm and an emission wavelength of 585-595 nm.

Needed but not supplied: Please download the kit booklet to verify if UltraPure Water (Milli-Q or equivalent) or any other components are needed for this assay.

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Technical Information
  • MPO Inhibitor Screening Assay Kit

Warning - this product is not for human or veterinary use.

Shipping & Storage
Wet ice in continental US; may vary elsewhere
≥ 1 year
Downloads & Resources
Product Downloads

Download Kit Booklet

Download Safety Data Sheet (SDS)

Download free InChI Key generation software

Additional Information

View the Cayman Structure Database for chemical structure definitions for many Cayman products

Get Batch-Specific Data and Documents by Batch Number

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data pack, and GC-MS data.

References & Product Citations
Product Description References

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).

7. Setsukinai, K.i., Urano, Y., Kakinuma, K., et al. Development of novel fluorescence probes that can reliably detect reactive oxygen species and distinguish specific species J. Biol. Chem. 278(5), 3170-3175 (2003).

Product Citations

Tao, L., Xu, M., Dai, X., et al. Polypharmacological profiles underlying the antitumor property of Salvia miltiorrhiza root (Danshen) interfering with NOX-dependent neutriphil extracellular traps Oxid. Med. Cell. Longev. 4908328, (2018).

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