Myeloperoxidase (MPO) antibody

Details for Product No. ABIN350505
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Antigen
Synonyms mpo, fj80f04, wu:fj80f04, MPO, LOC100335032, mKIAA4033
Reactivity
Human
(295), (50), (47), (24), (24), (12), (1), (1)
Host
Rabbit
(172), (143), (2), (1), (1), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(26), (17), (8), (5), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1)
Application
Immunohistochemistry (IHC), Western Blotting (WB)
(168), (163), (81), (50), (42), (29), (28), (27), (20), (17), (4), (3), (1), (1)
Pubmed 10 references available
Quantity 500 µg
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Catalog No. ABIN350505
454.67 $
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Immunogen Native myeloperoxidase isolated from human leucocytes
Isotype IgG
Specificity Specific for MPO.
Alternative Name MPO
Background 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.
Application Notes 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.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 500 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment 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.
Expiry Date 12 months
Supplier Images
anti-Myeloperoxidase (MPO) antibody 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
anti-Myeloperoxidase (MPO) antibody (2) 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
anti-Myeloperoxidase (MPO) antibody (3) 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).
General 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).

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