For immunochemical detection of MPO
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Myeloperoxidase (mouse) Polyclonal Antibody

Item No. 20493

Technical Information
Synonyms
  • MPO
Immunogen
Full-length recombinant mouse MPO
500 µl of protein A-purified polyclonal antibody
Storage Buffer
TBS, pH 7.4, with 50% glycerol, 0.1% BSA, and 0.02% sodium azide
Host
Rabbit
Applications
ELISA, IHC, WB
Species Reactivity
(+) Mouse; other species not tested
UniProt Accession №
P11247
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Myeloperoxidase (MPO) is a heme-containing enzyme and the most abundant protein in polymorphonuclear leukocytes (PMNs).1 It is composed of two subunits linked by a disulfide bridge with each subunit containing a light and a heavy polypeptide chain. It can oxidize a variety of substrates and catalyzes the formation of highly reactive (pseudo)hypohalous acids and radicals including hypochlorous acid. MPO is stored in azurophilic granules of PMNs and is released from activated or necrotic PMNs, after which it can bind to and modify acidic serum proteins, as well as recruit additional PMNs. MPO also has roles in PMN apoptosis and antimicrobial defense systems, including neutrophil extracellular traps (NETs).1,2,3 MPO-deficient mice exhibit reduced survival in a polymicrobial sepsis model, increased susceptibility to experimental autoimmune encephalomyelitis (EAE), and increased atherosclerosis in mice also deficient in the LDL receptor and fed an atherogenic diet.1,4,5 Cayman's Myeloperoxidase (mouse) Polyclonal Antibody can be used for ELISA, immunohistochemistry (IHC), and Western blot (WB) applications. The antibody recognizes MPO at approximately 80 kDa from mouse samples.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Arnhold, J., and Flemmig, J. Human myeloperoxidase in innate and acquired immunity. Arch. Biochem. Biophys. 500(1), 92-106 (2010).

    2. Metzler, K.D., Fuchs, T.A., Nauseef, W.M., et alMyeloperoxidase is required for neutrophil extracellular trap formation: Implications for innate immunity. Blood 117(3), 953-959 (2011).

    3. Urban, C.F., Ermert, D., Schmid, M., et alNeutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog. 5(10), e1000639 (2009).

    4. Brennan, M., Gaur, A., Pahuja, A., et alMice lacking myeloperoxidase are more susceptible to experimental autoimmune encephalomyelitis. J. Neuroimmunol. 112(1-2), 97-105 (2001).

    5. Brennan, M.L., Anderson, M.M., Shih, D.M., et alIncreased atherosclerosis in myeloperoxidase-deficient mice. J. Clin. Invest. 107(4), 419-430 (2001).