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Documentos Principais

ABS30

Sigma-Aldrich

Anti-Sulfenic Acid Modified Cysteine (2-Thiodimedone-Specific Ig) Antibody

serum, from rabbit

Sinônimo(s):

Sulfenic Acid Modified Cysteine (2-Thiodimedone-Specific Ig)

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About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Preço e disponibilidade não estão disponíveis no momento.

fonte biológica

rabbit

Nível de qualidade

forma do anticorpo

serum

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

reatividade de espécies

human, mouse, rat

reatividade da espécie (prevista por homologia)

all

técnica(s)

western blot: suitable

Isotipo

IgG

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Descrição geral

Protein sulfenic acid formation is a reversible post-translational modification that may be used to monitor protein oxidation on reactive cysteines within target proteins. This can be detected with protein sulfenic acid derivatised with dimedone.

Especificidade

This anitbody recognizes sulfenic acid modified proteins. Pan modification against all species.

Imunogênio

Linear peptide corresponding to sulfenic acid modified proteins.

Aplicação

Anti-Sulfenic Acid Modified Cysteine (2-Thiodimedone-Specific Ig) Antibody detects level of Sulfenic Acid Modified Cysteine & has been published & validated for use in WB.
Immunofluorescence Analysis: A previous lot was used by an independent laboratory in IF. (Seo, YH, et al. (2009). PNAS. 106(38): 16163-16168.)

Qualidade

Evaluated by Western Blot in rat ventricular myocyte lysate.

Western Blot Analysis: 01:1,000 dilution of this antibody detected sulfenic acid modified proteins on 10 µg of rat ventricular myocyte lysate.

Descrição-alvo

Pan antibody smear is expected.

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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1


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Ester Zito et al.
Molecular cell, 48(1), 39-51 (2012-09-18)
Endoplasmic reticulum (ER) thiol oxidases initiate a disulfide relay to oxidatively fold secreted proteins. We found that combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1α, ERO1β, and PRDX4 compromised the extracellular matrix in mice and interfered with
Phillip A Wages
Current protocols in toxicology, 71, 17-17 (2017-02-02)
Protein sulfenylation is a post-translational modification that is linked to many cell signaling networks and specific protein functions, thus the detection of any sulfenylated protein after a toxicological exposure is of importance. Specifically, the detection of protein sulfenylation can provide
Nikki L Jernigan et al.
PloS one, 12(6), e0180455-e0180455 (2017-07-01)
Pulmonary arterial hypertension is associated with a decreased antioxidant capacity. However, neither the contribution of reactive oxygen species to pulmonary vasoconstrictor sensitivity, nor the therapeutic efficacy of antioxidant strategies in this setting are known. We hypothesized that reactive oxygen species
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Molecular neurobiology, 53(8), 5229-5251 (2015-09-28)
Intracytoplasmic inclusions of protein aggregates in dopaminergic cells (Lewy bodies) are the pathological hallmark of Parkinson's disease (PD). Ubiquitin (Ub), alpha (α)-synuclein, p62/sequestosome 1, and oxidized proteins are the major components of Lewy bodies. However, the mechanisms involved in the

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