Myeloperoxidase (E1E7I) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) #49422
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Immunofluorescence (Immunocytochemistry) | 1:800 - 1:1600 |
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro734 of human myeloperoxidase protein.
Background
Myeloperoxidase (MPO) is a peroxidase enzyme that is part of the host defense system of polymorphonuclear leukocytes (reviewed in 1). The gene for MPO was cloned independently from several laboratories (2-5). A decrease in MPO expression was noticed upon differentiation of HL-60 cells (5). MPO catalyzes the reaction of hydrogen peroxide and chloride (or other halides) to produce hypochlorous acid and other potent antimicrobial oxidants. Knockout mice of MPO are impaired in clearing select microbial infections (6). Processing of mature MPO from an initial 80-90 kDa translation product involves insertion of a heme moiety, glycosylation, and proteolytic cleavage. The mature protein is a tetramer of two heavy chains (60 kDa) and two light chains (12 kDa). It is abundantly expressed in neutrophils and monocytes and secreted during their activation. Heightened MPO levels have been associated with tissue damage and a number of pathological conditions (1).
- Klebanoff, S.J. (2005) J Leukoc Biol 77, 598-625.
- Chang, K.S. et al. (1986) Blood 68, 1411-4.
- Yamada, M. et al. (1987) Arch Biochem Biophys 255, 147-55.
- Morishita, K. et al. (1987) J Biol Chem 262, 3844-51.
- Weil, S.C. et al. (1987) Proc Natl Acad Sci USA 84, 2057-61.
- Aratani, Y. et al. (2002) J Infect Dis 185, 1833-7.
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