| Clone: | CLB-MPO-1/1 |
|---|---|
| Isotype: | Mouse IgG2a |
| Specificity: | The mouse monoclonal antibody CLB-MPO-1/1 recognizes human myeloperoxidase, a heme protein present in myeloblasts, neutrophils and monocytes. 96% of all acute myelogenous leukemias were found positive and 100% of all acute lymphoblastic leukemias were found negative when staining with this antibody. |
| Immunogen: | Native purified human myeloperoxidase |
| Species Reactivity: | Human |
| Application: |
Flow Cytometry
Recommended dilution:1-5 μg/ml
Application note:intracellular staining
Immunocytochemistry
|
| Purity: | > 95% (by SDS-PAGE) |
| Purification: | Purified by protein A |
| Concentration: | 1 mg/ml |
| Storage Buffer: | Tris buffered saline (TBS) with 15 mM sodium azide, approx. pH 8.0 |
| Storage / Stability: | Store at 2-8°C. Do not use after expiration date stamped on vial label. For long-term storage aliquot and store at -20°C. Avoid freeze/thaw cycles. |
| Expiration: | See vial label |
| Lot Number: | See vial label |
| Background: | Myeloperoxidase (MPO) is a heme enzyme that is localized in azurophilic (primary) granules of myeloid cells and its synthesis occurs at an early stage of differentiation. The mature myeloperoxidase is a tetramer composed of two light (12 kDa) and two heavy (60 kDa) chains. This enzyme uses hydrogen peroxide to oxidize numerous substrates, including serotonin, melatonin or chloride, to produce reactive free radicals that contribute to immune reactions of myeloid cells against pathogens. Myeloperoxidase functions not only in host defense by mediating efficient microbial killing but also can contribute to progressive tissue damage in chronic inflammatory states such as atherosclerosis or acute pancreatitis. |
| References: |
*Hansson M, Olsson I, Nauseef WM: Biosynthesis, processing, and sorting of human myeloperoxidase. Arch Biochem Biophys. 2006 Jan 15;445(2):214-24.
*Ximenes VF, Maghzal GJ, Turner R, Kato Y, Winterbourn CC, Kettle AJ: Serotonin as a physiological substrate for myeloperoxidase and its
superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione. Biochem J. 2009 Dec 14;425(1):285-93.
*Ximenes VF, Silva SO, Rodrigues MR, Catalani LH, Maghzal GJ, Kettle AJ, Campa A: Superoxide-dependent oxidation of melatonin by myeloperoxidase. J Biol Chem. 2005 Nov 18;280(46):38160-9.
*Chooklin S, Pereyaslov A, Bihalskyy I: Pathogenic role of myeloperoxidase in acute pancreatitis. Hepatobiliary Pancreat Dis Int. 2009 Dec;8(6):627-31.
*Murphy EJ, Maréchal A, Segal AW, Rich PR: CO binding and ligand discrimination in human myeloperoxidase. Biochemistry. 2010 Mar 16;49(10):2150-8.
*van der Schoot CE, Daams GM, Pinkster J, Vet R, von dem Borne AE: Monoclonal antibodies against myeloperoxidase are valuable immunological reagents for the diagnosis of acute myeloid leukaemia. Br J Haematol. 1990 Feb;74(2):173-8.
*Garnache-Ottou F, Chaperot L, Biichle S, Ferrand C, Remy-Martin JP, Deconinck E, de Tailly PD, Bulabois B, Poulet J, Kuhlein E, Jacob MC, Salaun V, Arock M, Drenou B, Schillinger F, Seilles E, Tiberghien P, Bensa JC, Plumas J, Saas P: Expression of the myeloid-associated marker CD33 is not an exclusive factor for leukemic plasmacytoid dendritic cells. Blood. 2005 Feb 1;105(3):1256-64.
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