Human Myeloperoxidase/MPO Antibody

(1 citations)   
  • Species Reactivity
    Human
  • Specificity
    Detects human Myeloperoxidase/MPO in direct ELISAs and Western blots. In direct ELISAs, less than 30% cross-reactivity with recombinant mouse MPO is observed and less than 10% cross-reactivity with recombinant human Eosinophil Peroxidase (EPPO) is observed.
  • Source
    Polyclonal Goat IgG
  • Purification
    Antigen Affinity-purified
  • Immunogen
    Human polymorphonuclear leukocytes Myeloperoxidase and mouse myeloma cell line NS0-derived recombinant human Myeloperoxidase/MPO
    Ala49-Ser745
    Accession # P05164
  • Formulation
    Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
  • Label
    Unconjugated
Applications
  •  
    Recommended
    Concentration
    Sample
  • Western Blot
    0.5 µg/mL
    See below
  • Simple Western
    5 µg/mL
    See below
  • Immunocytochemistry
    5-15 µg/mL
    Immersion fixed HL‑60 human acute promyelocytic leukemia cell line
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Data Examples

Detection of Human Myeloperoxidase/MPO by Western Blot. Western blot shows lysates of HL‑60 human acute promyelocytic leukemia cell line and human neutrophil. PVDF membrane was probed with 0.5 µg/mL of Goat Anti-Human Myeloperoxidase/MPO Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3174) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Myeloperoxidase/MPO at approximately 60-65 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.

Detection of Human Myeloperoxidase/MPO by Simple WesternTM. Simple Western lane view shows lysates of human neutrophils, loaded at 0.2 mg/mL. A specific band was detected for Myeloperoxidase/MPO at approximately 65 kDa (as indicated) using 5 µg/mL of Goat Anti-Human Myeloperoxidase/MPO Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3174) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the
12-230 kDa separation system.

Preparation and Storage
  • Reconstitution
    Reconstitute at 0.2 mg/mL in sterile PBS.
  • Shipping
    The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
  • Stability & Storage
    Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
    • 12 months from date of receipt, -20 to -70 °C as supplied.
    • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
    • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Myeloperoxidase/MPO

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).

  • References:
    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.
  • Entrez Gene IDs:
    4353 (Human); 17523 (Mouse); 303413 (Rat)
  • Alternate Names:
    EC 1.11.1; EC 1.11.1.7; Lactoperoxidase; MPO; Myeloperoxidase
Related Research Areas
Citations:

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citations: Showing 1 - 1

  1. TLR9 Deficiency Leads to Accelerated Renal Disease and Myeloid Lineage Abnormalities in Pristane-Induced Murine Lupus
    Authors: L Bossaller, A Christ, K Pelka, K Nündel, PI Chiang, C Pang, N Mishra, P Busto, RG Bonegio, RE Schmidt, E Latz, A Marshak-Ro
    J. Immunol., 2016;197(4):1044-53.
    Species: Mouse
    Sample Type: Serum
    Application: ELISA Development
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