MPO antibody (PE)

Antigen: MPO

Clonality: Monoclonal (C2)

Host: Mouse

Reactivity: Human

Conjugate: PE

Application: Flow Cytometry (FACS), Immunofluorescence (IF)

Catalog no.: ABIN132140

Additional Information

Format: Purified

Isotype: IgG1

Clone: C2

Specificity: Myeloperoxidase (MPO) is a glycoprotein present in the azurophil (primary) granules of myeloid cells, which appears in the myeloblast stage of myeloid cell differentiation. MPO is he most common functional protein of myeloid cells and is involved in the inflammatory response. It helps to kill microbes by breaking down peroxide in the presence of halide ions, contributing to the bactericidal function of granulocytes. The primary translation product of MPO undergoes glycosylation with production of the 89 kDa heme-free apopro-MPO form followed by incorporation of heme and conversion into the enzymatically active pro-MPO form. Subsequently, pro-MPO becomes targeted to azurophil granules where final processing occurs to produce mature dimeric MPO consisting of the 59-64 kDa MPO ?-chain and the 14 kDa MPO ?-chain. The MPO-C2 mAb (clone 8E2) reacts with human myeloperoxidase (MPO) expressed by normal and malignant myelomonocytic cells.

Application Details

Application Notes: The MPO-C2 mAb (clone 8E6) recognizes virtually all myelomonocytic cells including AML blasts. The MPO-C2 mAb permits the identification and enumeration of myeloid cells in normal and malignant human blood and bone marrow using flow cytometry. Results must be put within the context of other diagnostic tests as well as the clinical history of the patient by a certified professional before final interpretation. Analyses performed with this antibody should be paralleled by positive and negative controls. If unexpected results are obtained which cannot be attributed to differences in laboratory procedures, please contact us. Sensitivity: The sensitivity of MPO-C2 mAb is determined by staining well-defined blood samples from representative donors with serial-fold mAb dilutions to obtain a titration curve that allows relating the mAb concentration to the percentage of stained cells and geometric MFI (mean fluorescence intensity). For this purpose, a mAb-concentration range is selected to include both the saturation point (i.e. the mAb dilution expected to bind all epitopes on the target cell) and the detection threshold (i.e. the mAb dilution expected to represent the least amount of mAb needed to detect an identical percentage of cells). In practice, 50 ?l of leukocytes containing 107cells/ml are stained with 20 ?l mAb of various dilutions to obtain a titration curve and to identify the saturation point and detection threshold. The final concentration of the product is then adjusted to be at least 3-fold above the detection threshold. In addition and to control lot-to-lot variation, the given lot is compared and adjusted to fluorescence standards with defined intensity.

Purification: Chromatography

Buffer: PBS pH 7.2, 1% BSA, 0.05% NaN3

Storage: For stability reasons this monoclonal antibody solution contains sodium azide. These reagents should be stored at 2-8

Restrictions: For Research Use. CE-certified for In Vitro Diagnostics (IVD) Use in the European Union

Images

anti-MPO antibody (PE)

Publications

Publications: Srivastava, Rado, Bauerle et al.: "Regulation of human bone marrow lactoferrin and myeloperoxidase gene expression by tumor necrosis factor-alpha." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 146, Issue 3, pp. 1014-9, 1991 (PubMed).

Nauseef: "Myeloperoxidase deficiency." in: Hematologic pathology, Vol. 4, Issue 4, pp. 165-78, 1991 (PubMed).

Catovsky, Matutes, Buccheri et al.: "A classification of acute leukaemia for the 1990s." in: Annals of hematology, Vol. 62, Issue 1, pp. 16-21, 1991 (PubMed).

Zaki, Austin, Swan et al.: "Human myeloperoxidase gene expression in acute leukemia." in: Blood, Vol. 74, Issue 6, pp. 2096-102, 1989 (PubMed).

Murao, Stevens, Ito et al.: "Myeloperoxidase: a myeloid cell nuclear antigen with DNA-binding properties." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, Issue 4, pp. 1232-6, 1988 (PubMed).

Nauseef, Olsson, Arnljots: "Biosynthesis and processing of myeloperoxidase--a marker for myeloid cell differentiation." in: European journal of haematology, Vol. 40, Issue 2, pp. 97-110, 1988 (PubMed).

Cramer, Pryzwansky, Villeval et al.: "Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold." in: Blood, Vol. 65, Issue 2, pp. 423-32, 1985 (PubMed).

Koeffler, Ranyard, Pertcheck: "Myeloperoxidase: its structure and expression during myeloid differentiation." in: Blood, Vol. 65, Issue 2, pp. 484-91, 1985 (PubMed).

Strobl, Takimoto, Majdic et al.: "Myeloperoxidase expression in CD34+ normal human hematopoietic cells." in: Blood, Vol. 82, Issue 7, pp. 2069-78, 1993 (PubMed).

Knapp, Majdic, Strobl: "Flow cytometric analysis of intracellular myeloperoxidase and lactoferrin in leukemia diagnosis." in: Recent results in cancer research. Fortschritte der Krebsforschung. Progrès dans les recherches sur le cancer, Vol. 131, pp. 31-40, 1993 (PubMed).

Gullberg, Andersson, Garwicz et al.: "Biosynthesis, processing and sorting of neutrophil proteins: insight into neutrophil granule development." in: European journal of haematology, Vol. 58, Issue 3, pp. 137-53, 1997 (PubMed).

Lanza, Latorraca, Moretti et al.: "Comparative analysis of different permeabilization methods for the flow cytometry measurement of cytoplasmic myeloperoxidase and lysozyme in normal and leukemic cells." in: Cytometry, Vol. 30, Issue 3, pp. 134-44, 1997 (PubMed).

Andersson, Hellman, Gullberg et al.: "The role of the propeptide for processing and sorting of human myeloperoxidase." in: The Journal of biological chemistry, Vol. 273, Issue 8, pp. 4747-53, 1998 (PubMed).

Imamura: "Sensitive detection technique of myeloperoxidase precursor protein by flow cytometry with monoclonal antibodies." in: American journal of hematology, Vol. 58, Issue 3, pp. 241-3, 1998 (PubMed).

Nakase, Sartor, Bradstock: "Detection of myeloperoxidase by flow cytometry in acute leukemia." in: Cytometry, Vol. 34, Issue 4, pp. 198-202, 1998 (PubMed).

Tsuruta, Tani, Hoshika et al.: "Myeloperoxidase gene expression and regulation by myeloid cell growth factors in normal and leukemic cells." in: Leukemia & lymphoma, Vol. 32, Issue 3-4, pp. 257-67, 1999 (PubMed).

Van, Schoonjans, Struijk et al.: "Influence of dialysate on gastric emptying time in peritoneal dialysis patients." in: Peritoneal dialysis international : journal of the International Society for Peritoneal Dialysis, Vol. 22, Issue 1, pp. 32-8, 2002 (PubMed).

Strobl, Knapp: "Myeloid cell-associated lysosomal proteins as flow cytometry markers for leukocyte lineage classification." in: Journal of biological regulators and homeostatic agents, Vol. 18, Issue 3-4, pp. 335-9, 2005 (PubMed).

Hipgrave, Tran, Huong et al.: "Immunogenicity of a locally produced hepatitis B vaccine with the birth dose stored outside the cold chain in rural Vietnam." in: The American journal of tropical medicine and hygiene, Vol. 74, Issue 2, pp. 255-60, 2006 (PubMed).