Recombinant Human Myeloperoxidase Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Enzyme Activity

Order Details

Recombinant Human Myeloperoxidase Protein, CF Summary

Details of Functionality
Measured by its ability to oxidize guaiacol in the presence of hydrogen peroxide. Capeillere-Blandin, C. (1998) Biochem J. 336 :395. The specific activity is >50,000 pmol/min/µg, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived human Myeloperoxidase/MPO protein
Ala49-Ser745, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Enzymes
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


  • Enzyme Activity
Theoretical MW
80 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
74-106 kDa, under reducing conditions.
Read Publications using
3174-MP in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 0.5-1 mg/mL in sterile, deionized water.
Assay Procedure
  • Assay Buffer: 50 mM NaH2PO4, pH 7.0
  • Recombinant Human Myeloperoxidase/MPO (rhMPO) (Catalog # 3174-MP)
  • Hydrogen Peroxide Solution, 30% (v/v) (H2O2) (Sigma, Catalog # H1009)
  • Guaiacol (Acros Organics, Catalog # AC120192500)
  • Clear StripWell Microplate (Costar, Catalog # 92592)
  • Plate Reader with Absorbance reading capability (Model: Spectramax Plus by Molecular Devices) or equivalent
  1. Prepare 100 mM guaiacol in Assay Buffer by shaking or stirring for 30 minutes at room temperature prior to use. Note: Protect guaiacol solution from light.
  2. Dilute rhMPO to 1 µg/mL in Assay Buffer.
  3. Dilute hydrogen peroxide from 30% to 0.00667% in Assay Buffer.
  4. Load in a clear microplate 20 µL of 1 µg/mL of rhMPO and 30 µL 0.00667% hydrogen peroxide, and start the reaction by adding 50 µL of 100 mM guaiacol.
  5. Read at 470 nm in kinetic mode for 5 minutes.
  6. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (OD/min) x Conversion Factor** (pmol/OD)
amount of enzyme (µg)

*Adjusted for Substrate Blank
**Derived using known concentrations of hydrogen peroxide ranging from 20 to 300 µM. Each point contains 10 µg/mL of rhMPO (an amount so that the reaction will be completed in a short period of time) and 50 mM guaiacol. After each reaction is complete, the product is measured at 470 nm (read endpoint about every 20 seconds to find the maximum absorbance for each point). The maximum values of Abs470 (y-axis) and pmol of hydrogen peroxide (x axis) for each point is plotted linearly (y = mx + b) and the slope is calculated (m). The conversion factor is derived from the following equation as a unit of pmol/OD. It is multiplied by 2 because one mol of hydrogen peroxide is equal to two mol of oxidized guaicol (product).

Conversion Factor = (1/slope(m)) x 2 = pmol/OD

Per Well:
  • rhMPO: 0.020 μg
  • Hydrogen Peroxide: 0.002%
  • Guaiacol: 50 mM


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Myeloperoxidase Protein, CF

  • EC 1.11.1
  • EC
  • MPO
  • Myeloperoxidase


Myeloperoxidase (MPO) is a heme-containing enzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein that catalyzes the hydrogen peroxide-dependent conversion of chloride, bromide, and iodide to multiple reactive species (1). Post-translational processing of MPO involves the insertion of a heme moiety and the proteolytic removal of both a propeptide and a 6 aa internal peptide (2). This results in a disulfide-linked dimer composed of a 60 kDa heavy and 12 kDa light chain that associate into a 150 kDa enzymatically active tetramer. The tetramer contains two heme groups and one disulfide bond between the heavy chains (2). Alternate splicing generates two additional isoforms of MPO, one with a 32 aa insertion in the light chain, and another with a deletion of the signal sequence and part of the propeptide (3). Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks (4‑6). Modification of ApoB100, as well as the lipid and cholesterol components of LDL and HDL, promotes the development of atherosclerosis (5, 7‑9). MPO is also associated with a variety of other diseases (1), and inhibits vasodilation in inflammation by depleting the levels of NO (10). Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells (11). MPO is stored in neutrophil azurophilic granules. Upon cellular activation, it is deposited into pathogen-containing phagosomes (2). While mice lacking MPO are impaired in clearing select microbial infections, MPO deficiency in humans does not necessarily result in heightened susceptibility to infections (12, 13).

  1. Klebanoff, S.J. (2005) J. Leukoc. Biol. 77:598.
  2. Hansson, M. et al. (2006) Arch. Biochem. Biophys. 445:214.
  3. Hashinaka, K. et al. (1988) Biochemistry 27:5906.
  4. van Dalen, C.J. et al. (2000) J. Biol. Chem. 275:11638.
  5. Hazen, S.L. and J.W. Heinecke (1997) J. Clin. Invest. 99:2075.
  6. Heinecke, J.W. et al. (1993) J. Clin. Invest. 91:2866.
  7. Podrez, E.A. et al. (1999) J. Clin. Invest. 103:1547.
  8. Bergt, C. et al. (2004) Proc. Natl. Acad. Sci. 101:13032.
  9. Hazen, S.L. et al. (1996) J. Biol. Chem. 271:23080.
  10. Eiserich, J.P. et al. (2002) Science 296:2391.
  11. Tiruppathi, C. et al. (2004) Proc. Natl. Acad. Sci. 101:7699.
  12. Aratani Y. et al. (2000) J. Infect. Dis. 182:1276.
  13. Kutter, D. (1998) J. Mol. Med. 76:669.

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Publications for Myeloperoxidase/MPO (3174-MP)(8)

We have publications tested in 3 confirmed species: Human, Bacteria - Staphylococcus aureus, N/A.

We have publications tested in 4 applications: Bioassay, Characterization, Enzyme Assay, Western Blot.

Filter By Application
Enzyme Assay
Western Blot
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Filter By Species
Bacteria - Staphylococcus aureus
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Showing Publications 1 - 8 of 8.
Publications using 3174-MP Applications Species
M Archer, P Dasari, D Walsh, KL Britt, A Evdokiou, WV Ingman Immune Regulation of Mammary Fibroblasts and the Impact of Mammographic Density Journal of Clinical Medicine, 2022;11(3):. 2022-01-01 [PMID: 35160252] (Bioassay, Human) Bioassay Human
AL Rozelle, Y Cheun, CK Vilas, MC Koag, S Lee DNA interstrand cross-links induced by the major oxidative adenine lesion 7,8-dihydro-8-oxoadenine Nature Communications, 2021;12(1):1897. 2021-01-01 [PMID: 33772030] (Bioassay, N/A) Bioassay N/A
EJ Tóth, M Varga, M Takó, M Homa, O Jáger, E Hermesz, H Orvos, G Nagy, C Vágvölgyi, T Papp Response of Human Neutrophil Granulocytes to the Hyphae of the Emerging Fungal Pathogen Curvularia lunata Pathogens, 2020;9(3):. 2020-01-01 [PMID: 32245253] (Bioassay, Human) Bioassay Human
NT Ploscariu, NWM de Jong, KPM van Kessel, JAG van Strijp, BV Geisbrecht Identification and structural characterization of a novel myeloperoxidase inhibitor from Staphylococcus delphini Arch. Biochem. Biophys., 2018;645(0):1-11. 2018-01-01 [PMID: 29524428] (Characterization, Bacteria - Staphylococcus aureus) Characterization Bacteria - Staphylococcus aureus
NWM de Jong, NT Ploscariu, KX Ramyar, BL Garcia, AI Herrera, O Prakash, BB Katz, KG Leidal, WM Nauseef, KPM van Kessel, JAG van Strijp, BV Geisbrecht A Structurally Dynamic N-terminal Region Drives Function of the Staphylococcal Peroxidase Inhibitor (SPIN) J. Biol. Chem., 2018;0(0):. 2018-01-01 [PMID: 29306874] (Bioassay, N/A) Bioassay N/A
NWM de Jong, KX Ramyar, FE Guerra, R Nijland, C Fevre, JM Voyich, AJ McCarthy, BL Garcia, KPM van Kessel, JAG van Strijp, BV Geisbrecht, PA Haas Immune evasion by a staphylococcal inhibitor of myeloperoxidase Proc. Natl. Acad. Sci. U.S.A., 2017;0(0):. 2017-01-01 [PMID: 28808028] (Bioassay, Bacteria - Staphylococcus aureus) Bioassay Bacteria - Staphylococcus aureus
Gut Microbiota Conversion of Dietary Ellagic Acid into Bioactive Phytoceutical Urolithin A Inhibits Heme Peroxidases PLoS ONE, 2016;11(6):e0156811. 2016-01-01 [PMID: 27254317] (Enzyme Assay, Human) Enzyme Assay Human
Huang S, Feng C, Hung H, Chakraborty C, Chen C, Chen W, Jean Y, Wang H, Sung C, Sun Y, Wu C, Liu W, Hsiao C, Wen Z A novel zebrafish model to provide mechanistic insights into the inflammatory events in carrageenan-induced abdominal edema. PLoS ONE, 2014;9(8):e104414. 2014-01-01 [PMID: 25141004] (Western Blot, N/A) Western Blot N/A

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Gene Symbol MPO