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ABS30

Sigma-Aldrich

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

serum, from rabbit

Synonym(s):

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

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, mouse, rat

species reactivity (predicted by homology)

all

technique(s)

western blot: suitable

isotype

IgG

shipped in

wet ice

target post-translational modification

unmodified

General description

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.

Specificity

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

Immunogen

Linear peptide corresponding to sulfenic acid modified proteins.

Application

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.)

Quality

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 Āµg of rat ventricular myocyte lysate.

Target description

Pan antibody smear is expected.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1


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 productā€™s label following the words ā€˜Lotā€™ or ā€˜Batchā€™.

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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 ERO1Ī±, ERO1Ī², and PRDX4 compromised the extracellular matrix in mice and interfered with
Nannan Zhou et al.
The Journal of clinical investigation, 133(24) (2023-12-15)
Elevation of reactive oxygen species (ROS) levels is a general consequence of tumor cells' response to treatment and may cause tumor cell death. Mechanisms by which tumor cells clear fatal ROS, thereby rescuing redox balance and entering a chemoresistant state
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
Juliana Navarro-Yepes et al.
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 (Ī±)-synuclein, p62/sequestosome 1, and oxidized proteins are the major components of Lewy bodies. However, the mechanisms involved in the
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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