N5787
Anti-Neutrophil Myeloperoxidase antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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About This Item
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
indirect ELISA: 1:4,000
western blot: 1:4,000
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MPO(4353)
General description
Myeloperoxidase (MPO) is an oxidoreductase which is part of the heme peroxidase superfamily.
Immunogen
human neutrophil myeloperoxidase.
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)
Enzyme-linked immunosorbent assay (1 paper)
Biochem/physiol Actions
Myeloperoxidase (MPO) is present in the neutrophils and released when leukocytes are activated. It takes part in defense mechanisms and oxidizes low-density lipoprotein. MPO possesses a chlorinating activity with which it generates hypochlorous acid (an anti-microbial agent). It also decreases the bioavailability of nitric oxide.
Physical form
Solution in phosphate buffered saline and 0.05% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Judit Kalász et al.
Free radical biology & medicine, 84, 116-127 (2015-03-17)
We set out to characterize the mechanical effects of myeloperoxidase (MPO) in isolated left-ventricular human cardiomyocytes. Oxidative myofilament protein modifications (sulfhydryl (SH)-group oxidation and carbonylation) induced by the peroxidase and chlorinating activities of MPO were additionally identified. The specificity of
Matthew J Gounis et al.
Stroke, 45(5), 1474-1477 (2014-04-10)
Noninvasive imaging identifying a predictive biomarker of the bleeding risk of unruptured intracranial aneurysms (UIAs) is needed. We investigated a potential biomarker of UIA instability, myeloperoxidase, in human aneurysm tissue. Human brain aneurysms were harvested after clipping and were histologically
Pierre-Louis Leger et al.
Experimental neurology, 230(1), 58-66 (2010-07-06)
The effects of ischemia-reperfusion on opening of the mitochondrial permeability transition pore (mPTP) and its blockade in the immature brain are not fully understood. Presently, we evaluated the effect of cyclosporine A (CsA) on cell death and mPTP opening in
Peng-cheng Xu et al.
BMC immunology, 16, 10-10 (2015-04-17)
C-reactive protein (CRP) exerts prothrombotic effects through dissociating from pentameric CRP (pCRP) into modified or monomeric CRP (mCRP). However, although the high prevalence of venous thromboembolism (VTE) in patients with anti-neutrophil cytoplasmic antibody (ANCA)-associated vasculitis (AAV) has been identified, it
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