Myeloperoxidase (MPO) antibody

Antigen: Myeloperoxidase (MPO)

Synonyms: KIAA4033, mKIAA4033, mpo, fj80f04, wu:fj80f04, MPO, LOC100335032

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350505

Additional Information

UniProt: P05164

Immunogen: Native myeloperoxidase isolated from human leucocytes

Format: Lyophilized

Isotype: IgG

Description: Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of netrophils. SUBCELLULAR LOCATION: Lysosome Also known as: MPO.

Specificity: Appears to be specific for MPO.

Application Details

Application Notes: IHC, WB. A working concentration of 10-50 µg/ml is recommended. The optimal dilution should be determined by the end user. This antibody performs superbly in paraffin-embedded tissue sections fixed in formalin, frozen sections and cell cytospins.

Purity: IgG

Purification: Rabbit Anti-EGFR (Phospho-Tyr1172) Polyclonal Antibody is affinity-purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide is removed by chromatogramphy using non-phosphopeptide corresponding to the phosphorylation site.

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Research Area: Enzymes, Metabolism, Immunology

Restrictions: For Research Use only

Images

Isolated monocytes were stained with Lysotrack red followed by staining with Rabbit antibody to human myeloperoxidase (MPO): IgG (3µg/ml) for 1 hour at room temperature, washed and  followed by staining with goat anti-rabbit antibody conjugated to Alexa 488 (Green) for 1 hr. Mounting media (10% Glycerol in PBS) containing Hoechst 33258 1 µg/ml (Sigma-Aldrich) was used for nuclear counterstaining (Blue).  Fluorescent cell staining was analysed by confocal microscopy using a BioRad Radiance 2100 confocal microscope. Magnification: 80X

Isolated monocytes were stained with Lysotrack red followed by staining with Rabbit antibody to human myeloperoxidase (MPO): IgG (3µg/ml) for 1 hour at room temperature, washed and followed by staining with goat anti-rabbit antibody conjugated to Alexa 488 (Green) for 1 hr. Mounting media (10% Glycerol in PBS) containing Hoechst 33258 1 µg/ml (Sigma-Aldrich) was used for nuclear counterstaining (Blue). Fluorescent cell staining was analysed by confocal microscopy using a BioRad Radiance 2100 confocal microscope. Magnification: 200X

10 µg of neutrophil lysate was separated by 12% SDS-PAGE. Proteins were transferred onto a PVDF membrane and blocked by incubation with PBS containing 2% skim milk and 0.02% Tween 20 for 30 min. Membranes were probed with Rabbit antibody to human myeloperoxidase (MPO): IgG (3 µg/ml) for 1 hr. Membranes were then probed with goat anti-rabbit antibody conjugated to alkaline phosphatase diluted 1:1000 and developed with ECF luminescence substrate (Amersham Biosciences).

Publications

Hashinaka, Nishio, Hur et al.: "Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation." in: Biochemistry, Vol. 27, Issue 16, pp. 5906-14, 1989 (PubMed).

Morishita, Kubota, Asano et al.: "Molecular cloning and characterization of cDNA for human myeloperoxidase." in: The Journal of biological chemistry, Vol. 262, Issue 8, pp. 3844-51, 1987 (PubMed).

Johnson, Nauseef, Care et al.: "Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species." in: Nucleic acids research, Vol. 15, Issue 5, pp. 2013-28, 1987 (PubMed).

Seto, Hirayu, Magnusson et al.: "Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase." in: The Journal of clinical investigation, Vol. 80, Issue 4, pp. 1205-8, 1987 (PubMed).

Hosokawa, Kawaguchi, Hikiji et al.: "Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1." in: Leukemia : official journal of the Leukemia Society of America, Leukemia Research Fund, U.K, Vol. 7, Issue 3, pp. 441-5, 1993 (PubMed).

Yamada, Yoshida, Hashinaka: "Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene." in: The Journal of biological chemistry, Vol. 268, Issue 18, pp. 13479-85, 1993 (PubMed).

Fiedler, Davey, Fenna: "X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution." in: The Journal of biological chemistry, Vol. 275, Issue 16, pp. 11964-71, 2000 (PubMed).

Liu, Qian, Gritsenko et al.: "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." in: Journal of proteome research, Vol. 4, Issue 6, pp. 2070-80, 2005 (PubMed).

Ramachandran, Boontheung, Xie et al.: "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." in: Journal of proteome research, Vol. 5, Issue 6, pp. 1493-503, 2006 (PubMed).

Sjöblom, Jones, Wood et al.: "The consensus coding sequences of human breast and colorectal cancers." in: Science (New York, N.Y.), Vol. 314, Issue 5797, pp. 268-74, 2006 (PubMed).