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N5787

Sigma-Aldrich

Anti-Neutrophil Myeloperoxidase antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

IgG fraction of antiserum

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

reatividade de espécies

human

técnica(s)

indirect ELISA: 1:4,000
western blot: 1:4,000

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... MPO(4353)

Descrição geral

Myeloperoxidase (MPO) is an oxidoreductase which is part of the heme peroxidase superfamily.

Imunogênio

human neutrophil myeloperoxidase.

Aplicação

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Enzyme-linked immunosorbent assay (1 paper)

Ações bioquímicas/fisiológicas

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.

forma física

Solution in phosphate buffered saline and 0.05% sodium azide.

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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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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