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PE Mouse Anti-Human Myeloperoxidase (MPO)
Product Details
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BD™
Human
Mouse IgG1, κ
Intracellular staining (flow cytometry)
3 μg/mL
20 μL
4353
AB_400235
Phosphate buffered saline with gelatin and 0.1% sodium azide.
RUO (GMP)


Preparation And Storage

The FITC conjugate is supplied as 12.5 µg in 1.0 mL (12.5 µg/mL) of PBS. The PE conjugate is supplied as 3 µg in 1.0 mL (3 µg/mL) of PBS. PBS contains gelatin and 0.1% sodium azide. Vials should be stored at 2° to 8°C. Conjugated forms should not be frozen and should be protected from prolonged exposure to light. Each reagent is stable for the period shown on the bottle label when stored as directed.

341642 Rev. 1
Antibody Details
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5B8

Anti-MPO, clone 5B8, is generated from the fusion of X63.Ag8-653 myeloma cells with spleen cells from BALB/c mice immunized with commercially purified myeloperoxidase.

The Anti-Myeloperoxidase (MPO) antibody reacts with intracellular MPO, aconsisting of two molecular subunits, 60 kilodaltons (kDa) and 12 kDa.5is a major enzyme involved in the inflammatory responses of polymorphonuclear. It catalyzes the production of hypochlorous acid, a potent microbicidal.

341642 Rev. 1
Format Details
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PE
R-Phycoerythrin (PE), is part of the BD family of Phycobiliprotein dyes. This fluorochrome is a multimeric fluorescent phycobiliprotein with excitation maximum (Ex Max) of 496 nm and 566 nm and an emission maximum (Em Max) at 576 nm. PE is designed to be excited by the Blue (488 nm), Green (532 nm) and Yellow-Green (561 nm) lasers and detected using an optical filter centered near 575 nm (e.g., a 575/26-nm bandpass filter). As PE is excited by multiple lasers, this can result in cross-laser excitation and fluorescence spillover on instruments with various combinations of Blue, Green, and Yellow-Green lasers. Please ensure that your instrument’s configurations (lasers and optical filters) are appropriate for this dye.
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PE
Yellow-Green 488 nm, 532 nm, 561 nm
496 nm, 566 nm
576 nm
341642 Rev.1
Citations & References
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Development References (6)

  1. Audrain MA, Baranger TA, Moguilevski N, et al. Anti-native and recombinant myeloperoxidase monoclonals and human autoantibodies. Clin Exp Immunol. 1997; 107(1):127-134. (Biology). View Reference
  2. Grégoire C, Welch H, Astarie-Dequeker C, Maridonneau-Parini I. Expression of azurophil and specific granule proteins during differentiation of NB4 cells in neutrophils. J Cell Physiol. 1998; 175:203-210. (Biology).
  3. Knapp W, Strobl H, Majdic O. Flow cytometric analysis of cell-surface and intracellular antigens in leukemia diagnosis. Cytometry. 1994; 18(4):187-198. (Biology). View Reference
  4. Nauseef WM, Malech HL. Analysis of the peptide subunits of human neutrophil myeloperoxidase. Blood. 1986; 5:1504-1507. (Biology).
  5. Scheinecker C, Strobl H, Fritsch G, et al. Granulomonocyte-associated lysosomal protein expression during in vitro expansion and differentiation of CD34+ hematopoietic progenitor cells. Blood. 1995; 86:4115-4123. (Biology).
  6. Tobler A, Miller CW, Johnson KR, Selsted ME, Rovera G, Koeffler HP. Regulation of gene expression of myeloperoxidase during myeloid differentiation. J Cellular Physiol. 1988; 136:215-225. (Biology).
View All (6) View Less
341642 Rev. 1

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