N5787
Anti-Neutrophil Myeloperoxidase antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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About This Item
Produtos recomendados
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)
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
Certificados de análise (COA)
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Martin T Spang et al.
Nature biomedical engineering, 7(2), 94-109 (2022-12-30)
Decellularized extracellular matrix in the form of patches and locally injected hydrogels has long been used as therapies in animal models of disease. Here we report the safety and feasibility of an intravascularly infused extracellular matrix as a biomaterial for
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
Ishan Agrawal et al.
STAR protocols, 2(3), 100678-100678 (2021-08-07)
Extracellular traps (ETs) are composed of decondensed chromatin and are embedded with various antimicrobial proteins like myeloperoxidase and histones. Recently, we reported that dopamine (DA) induces ETs in BV2 microglia cell line and primary adult human microglia in a manner
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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