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Merck

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

origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

IgG fraction of antiserum

tipo de anticuerpo

primary antibodies

clon

polyclonal

formulario

buffered aqueous solution

reactividad de especies

human

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... MPO(4353)

Descripción general

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

Inmunógeno

human neutrophil myeloperoxidase.

Aplicación

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

Acciones bioquímicas o 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.

Cláusula de descargo de responsabilidad

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 clase de almacenamiento

10 - Combustible liquids

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°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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