Human Myeloperoxidase (MPO)
Native, whole molecule, biologically active
Produktdetails
Synonyms
MPO
Description of Human Myeloperoxidase (MPO)
Human Myeloperoxidase (MPO) is a 130000-150000 Da protein. Myeloperoxidase (MPO) is a heme-containing enzyme predominantly found in neutrophil granules, where it plays a crucial role in the innate immune response. MPO catalyzes the oxidation of chloride ions by hydrogen peroxide to produce hypochlorous acid (HOCl), a potent antimicrobial agent that destroys bacteria, viruses, and tumor cells within phagolysosomes during phagocytosis. This enzyme’s unique structure, including a sulfonium linkage in its heme group, grants it high oxidizing potential and enables it to oxidize a broad range of substrates, such as amino acids, thiols, and steroid hormones, through both halogenation and peroxidase cycles. In addition to direct microbicidal activity, MPO can inactivate chemotactic factors, crosslink proteins, and modify biomolecules, which contributes to the regulation of inflammation and immune signaling. However, excessive or misdirected MPO activity is implicated in chronic inflammatory diseases, including atherosclerosis, neurodegenerative disorders, arthritis, and cancer, due to tissue damage from reactive oxidants. Clinically, MPO serves as both a biomarker and a potential therapeutic target in cardiovascular and inflammatory diseases, and its selective cytotoxicity is being explored for antiseptic and anticancer applications.
Source
Neutrophils shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
Biological Activity
> 200 units/mg protein after lyophilization. One unit is defined as the amount of enzyme that decomposes 1 µmol of hydrogen peroxide/min at 25 °C, pH 6.1. Reaction mixture contains 30 mM sodium phosphate, pH 6.1, 30 mM guaiacol, and 0.0012% (0.35 mM) hydrogen peroxide.
Storage
For long term, store Human Myeloperoxidase (MPO) at ≤ -20°C.
Applications
In Vitro Diagnostics, Vasculitis, Autoimmune Diseases, Antigen Production, Assay Standards, Infection, Inflammation, Cancer.
Citations/Publications
Martin, C., et al., (2019), 'A Biodegradable Multifunctional Graphene Oxide Platform for Targeted Cancer Therapy', Adv. Funct. Mater. 29: pp 1901761. Available at: https://doi.org/10.1002/adfm.201901761
Yan, Z., et al., (2024), 'Nanobiology Dependent Therapeutic Convergence between Biocompatibility and Bioeffectiveness of Graphene Oxide Quantum Dot Scaffold for Immuno-Inductive Angiogenesis and Nerve Regeneration', Adv. Funct. Mater. 33: 2211709, Available at: DOI: 10.1002/adfm.202211709
Lin, H., et al., (2017), 'A Two-Dimensional Biodegradable Niobium Carbide (MXene) for Photothermal Tumor Eradication in NIR‑I and NIR-II Biowindows', J. Am. Chem. Soc. 139: pp 16235-16247. Available at: DOI: 10.1021/jacs.7b07818
Harboe, M., et al., (2017), 'Properdin binding to complement activating surfaces depends on initial C3b deposition', PNAS, 114(4): pp E534-E53. Available at: https://doi.org/10.1073/pnas.1612385114
McCall, A. S., et al., (2018), 'Inhibitory Anti-Peroxidasin Antibodies in Pulmonary-Renal Syndromes', J Am Soc Nephrol 29: pp 2619–2625. Available at: doi: https://doi.org/10.1681/ASN.2018050519
NCBI: https://www.ncbi.nlm.nih.gov/protein/P05164/
Shipped with ice packs
Gel Scan of Human Myeloperoxidase (MPO)
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
Paying by bank transfer
