Mpo antibody

Manufactured by Thermo Fisher Scientific

Sourced in United Kingdom

The MPO antibody is a laboratory reagent used for the detection and identification of the myeloperoxidase protein in biological samples. It is a specific immunological probe that can be utilized in various analytical techniques to study the presence and distribution of myeloperoxidase, an enzyme found in certain white blood cells.

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Lab products found in correlation

Foxp3 antibody, by Cell Signaling Technology (1 mentions) F4 80 antibody, by Cell Signaling Technology (1 mentions) 3 3 diaminobenzidine (dab), by Nichirei Biosciences (1 mentions)

Close spelling variants of this product

Anti-MPO antibody (7 citations) Anti-myeloperoxidase (MPO) antibody (3 citations) Antihuman MPO antibody (3 citations) Rabbit polyclonal antibody against MPO (2 citations)

4 protocols using mpo antibody

Tissue Microarray and Immunohistochemistry Protocol

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The Ethics Committee of the Kanton St. Gallen, Switzerland, approved all procedures involving human materials used in this St. Gallen tissue microarray (TMA), and each patient signed an informed consent. The construction of TMA and IHC procedures have been was described previously (Guo et al., 2018). The POSTN antibody was from Abcam (Cambridge, MA, USA; ab14041). The MPO antibody was from NeoMarkers/Lab Vision Corporation (Thermo Fisher Scientific, Cheshire, UK; RB‐373‐A1).

Zhu Y., Weiss T., Zhang Q., Sun R., Wang B., Yi X., Wu Z., Gao H., Cai X., Ruan G., Zhu T., Xu C., Lou S., Yu X., Gillet L., Blattmann P., Saba K., Fankhauser C.D., Schmid M.B., Rutishauser D., Ljubicic J., Christiansen A., Fritz C., Rupp N.J., Poyet C., Rushing E., Weller M., Roth P., Haralambieva E., Hofer S., Chen C., Jochum W., Gao X., Teng X., Chen L., Zhong Q., Wild P.J., Aebersold R, & Guo T. (2019). High‐throughput proteomic analysis of FFPE tissue samples facilitates tumor stratification. Molecular Oncology, 13(11), 2305-2328.

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Gastric Immune Cell Quantification

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Paraffin-embedded gastric tissues from five control mice, four C. acnes-colonized mice, and eight mice from H. pylori and coinfected groups were stained using F4/80 antibody (1:100, Cell Signaling Technology, Danvers, MA) to detect macrophages, CD3 antibody (1:400, Agilent Dako, Santa Clara, CA) to detect T cells, FOXP3 antibody (1:100, Cell Signaling Technology, Danvers, MA) to detect Treg cells, CD45 B220 antibody (1:400, Thermo Scientific, Waltham, MA) to detect B cells, and MPO antibody (1:50, Thermo Scientific, Waltham, MA) to detect neutrophils by immunohistochemistry as previously described (5 (link)). Positive cells as a percentage of total cells within the gastric mucosa of whole digital slides were quantified using QuPath imaging software.

Lunger C., Shen Z., Holcombe H., Mannion A.J., Dzink-Fox J., Kurnick S., Feng Y., Muthupalani S., Carrasco S.E., Wilson K.T., Peek R.M., Piazuelo M.B., Morgan D.R., Armijo A.L., Mammoliti M., Wang T.C, & Fox J.G. (2023). Gastric coinfection with thiopeptide-positive Cutibacterium acnes decreases FOXM1 and pro-inflammatory biomarker expression in a murine model of Helicobacter pylori-induced gastric cancer. Microbiology Spectrum, 12(1), e03450-23.

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Quantification of Inflammatory Changes in Pancreatitis

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Quantification of inflammatory cell infiltration and vacuolization was performed on H&E stained pancreatic tissue (7 hourly cerulein injections or L-arginine model) sections from 4–5 mice per group and expressed as the number of inflammatory cells or vacuoles per 100 acinar cells. For cerulein-induced pancreatitis, neutrophil infiltration in pancreas was further quantified in pancreatic tissue sections stained with myeloperoxidase (MPO) antibody (Thermo Fisher Scientific, Rockford, IL) by immunohistochemical staining. Pancreatic edema was evaluated by grading from 0–3 according to Schoenberg grading system [45 (link)] and by measuring the wet-to-dry weight ratio as described [46 (link),26 (link)].

Yuan J., Chheda C., Piplani H., Geng M., Tan G., Thakur R, & Pandol S.J. (2020). Pancreas-specific deletion of protein kinase D attenuates inflammation, necrosis, and severity of acute pancreatitis. Biochimica et biophysica acta. Molecular basis of disease, 1867(1), 165987.

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Immunostaining of TGFβ1 and Cell Markers in Tissue Samples

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Deparaffinized sections were processed for immunohistochemistry as previously reported (Saika et al. 2005a (link), b (link)). Antibodies used are listed in Table 1. Antibody-specific tissue antigen interactions were identified based on peroxidase-conjugated secondary antibody reactions visualized with 3,3′-diaminobenzidine (Nichirei Biosciences, Tokyo, Japan) and nuclei counterstaining with methylgreen. Secreted active form of TGFβ1 was immunostained as previously reported with a specific antibody produced by us (Flanders et al. 1991 (link); Flanders et al. 1989 (link)). Specimens were observed under light microscopy (BX50, Olympus, Tokyo, Japan).Table 1

Antibodies used

Rabbit polyclonal anti-TRPV1 antibody (1:500; Neuromics)
Mouse monoclonal anti-α-SMA antibody (1:200; Neomarker, Fremont, CA)
Rabbit polyclonal anti-SM22 alpha antibody (1:200; Abcam, Cambridge, UK)
Rabbit polyclonal MPO antibody (1:100; Thermo scientific, Fremont, CA)
Rat monoclonal anti-macrophage F4/80 antibody (1:50; BMA Biomedicals, August, Switzerland)
Active form of TGFβ1 antibody (Flanders et al. 1989 (link))

TRPV1 transient receptor potential vanilloid subtype 1, αSMA α-smooth muscle actin, MPO myeloperoxidase

Nidegawa-Saitoh Y., Sumioka T., Okada Y., Reinach P.S., Flanders K.C., Liu C.Y., Yamanaka O., Kao W.W, & Saika S. (2018). Impaired healing of cornea incision injury in a TRPV1-deficient mouse. Cell and Tissue Research, 374(2), 329-338.

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