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Myeloperoxidase Rabbit mAb
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Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P05164 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Monoclonal Antibody |
| Isotype | IgG |
| Conjugate | Unconjugated |
| Purification | Affinity Purified |
| Calculated MW | 83869 Da |
| Gene ID | 4353 |
|---|---|
| Other Names | MPO |
| Dilution | WB~~1:1000-1:5000 IHC-P~~1:50~200 |
| Format | Liquid in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA. |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | MPO {ECO:0000303|PubMed:21880720, ECO:0000312|HGNC:HGNC:7218} |
|---|---|
| Function | Peroxidase that plays a central role in the host defense system of polymorphonuclear leukocytes by mediating both (1) formation of neutrophil extracellular trap (NETs) and (2) microbicidal activity (PubMed:16125131, PubMed:17438335, PubMed:20974672, PubMed:20974816, PubMed:22131345, PubMed:25066128, PubMed:28574339, PubMed:40963017, PubMed:4978299, PubMed:6295491). Promotes NET formation by mediating chromatin disassembly: translocates to the nucleus and specifically binds to nucleosomes, both as monomer and homodimer, leading to nucleosome unstacking and initial chromatin decondensation (PubMed:40963017). Homodimers clash with one end of the nucleosomal DNA, leading to DNA unwrapping, initiating complete disassembly of nucleosomes and chromatin transformation into NETs in an ATP- independent manner (PubMed:40963017). NETs, which are mainly composed of DNA fibers and globular proteins, are then extruded into the extracellular space by neutrophils to trap pathogens and release antimicrobial proteins to destroy them (PubMed:40963017). Participates to the microbicidal activity against a wide range of organisms by acting as a peroxidase that catalyzes the formation of oxidants in presence of hydrogen peroxide (PubMed:16125131, PubMed:17074761, PubMed:17438335, PubMed:21880720, PubMed:22131345, PubMed:22352991, PubMed:22902565, PubMed:24194519, PubMed:33273015, PubMed:9359420, PubMed:9922160). Mediates the formation of hypohalous acids, mainly hypochlorous acid (HOCl) in physiologic situations, that greatly enhance polymorphonuclear leukocyte microbicidal activity (PubMed:16125131, PubMed:17074761, PubMed:17438335, PubMed:19608745, PubMed:21880720, PubMed:22902565, PubMed:24194519, PubMed:9359420, PubMed:9922160). In addition to hypochlorous acid, catalyzes formation of hypobromous acid (HOBr), hypoiodous acid (HOI) and hypothiocyanous acid (HOSCN) (PubMed:1318692, PubMed:16125131, PubMed:17438335, PubMed:19608745, PubMed:6295491, PubMed:9359420). Also catalyzes oxidation of nitrite into the highly reactive nitrogen dioxide radical (PubMed:10777476, PubMed:8385644, PubMed:9450756). Formation of oxidants are widely believed to be responsible for much of the anti- bactericidal activity of neutrophils (PubMed:8385644, PubMed:9450756). Oxidants, such as hypochlorous acid or nitrogen dioxide radical, can also oxidize amino acid residues on proteins and generate chlorination and nitration post-translational modifications, respectively (PubMed:15314690, PubMed:15326314, PubMed:15498770, PubMed:15574409, PubMed:16091367, PubMed:7622459). Chlorination and nitration of the lipid-free form of APOA1 impairs cholesterol transport (PubMed:15326314, PubMed:15498770, PubMed:15574409). Superoxides generated by MPO can also promote dioxygenation of tryptophan residues on proteins (PubMed:16091367, PubMed:40081572). Also able to oxidize melatonin into N1-acetyl-N2-formyl-5-methoxykynuramine either in presence of hydrogen peroxide or superoxide (PubMed:15636586, PubMed:16148002). Oxidizes urate into 5-hydroxyisourate (PubMed:21266577). Functions as a nitric oxide (NO) oxidase during inflammation, by catalytically consuming NO, impairing NO's ability to maintain vascular tone and function (PubMed:12089442). May also mediate the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1- microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (PubMed:25698971). |
| Cellular Location | Lysosome. Cytolytic granule. Cytoplasmic vesicle, phagosome. Secreted. Nucleus. Chromosome Note=Localizes to azurophil granules, a type of primary lysosome found in neutrophils and monocytes that contains antimicrobial proteins (PubMed:25066128, PubMed:2981589, PubMed:6095812, PubMed:6192815). A substantial fraction is also constitutively secreted by normal bone marrow granulocyte precursors (PubMed:6095812). During formation of neutrophil extracellular traps (NETs), translocates into the nucleus and associates to chromatin, leading to chromatin dislocation and its transformation into NETs (PubMed:25066128, PubMed:40963017). Core component of NETs (PubMed:22131345, PubMed:32434865, PubMed:40963017) |
| Tissue Location | Specifically expressed in neutrophils and monocytes. |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Myeloperoxidase (MPO) is a peroxidase enzyme that is part of the host defense system of polymorphonuclear leukocytes. Heightened MPO levels have been associated with tissue damage and a number of pathological conditions.
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