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927813

Sigma-Aldrich

PFPSA-alkyne

≥95%

Synonym(e):

N-(But-3-yn-1-yl)-2,3,4,5,6-pentafluorobenzenesulfonamide

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About This Item

Empirische Formel (Hill-System):
C10H6F5NO2S
Molekulargewicht:
299.22
UNSPSC-Code:
12352101
NACRES:
NA.22

Qualitätsniveau

100

Assay

≥95%

Form

powder

Lagertemp.

−20°C

Anwendung

PFPSA-alkyne is a probe that can be used to label cysteines through nucleophilic aromatic substitution. A method was developed using cysteine-reactive compounds including this one to allow for unbiased analysis of proteomic data in quantitave applications (Zanon et al. 2021). The method uses light or heavy labeling with the isotopically labelled desthiobiotin azide (isoDTB) tag for mass spectrometry analysis (Zanon et al. 2020). Analysis then uses the isotopic tandem orthogonal proteolysis activity-based protein profiling (isoTOP-ABPP) workflow (Weerapana et al. 2010, Backus et al. 2016).

Piktogramme

Exclamation mark
GHS07

Signalwort

Warning

H-Sätze

H315,H319

Gefahreneinstufungen

Eye Irrit. 2 - Skin Irrit. 2

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

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Profiling the proteome-wide selectivity of diverse electrophiles.
Zanon P R A, et al.
ChemRxiv : the preprint server for chemistry (2021)
Eranthie Weerapana et al.
Nature, 468(7325), 790-795 (2010-11-19)
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tuned to perform diverse biochemical functions. The absence of a consensus sequence that defines functional cysteines in proteins has hindered their discovery and characterization. Here we
Patrick R A Zanon et al.
Angewandte Chemie (International ed. in English), 59(7), 2829-2836 (2019-11-30)
Rapid development of bacterial resistance has led to an urgent need to find new druggable targets for antibiotics. In this context, residue-specific chemoproteomic approaches enable proteome-wide identification of binding sites for covalent inhibitors. Described here are easily synthesized isotopically labeled
Eranthie Weerapana et al.
Nature, 468(7325), 790-795 (2010-11-19)
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tuned to perform diverse biochemical functions. The absence of a consensus sequence that defines functional cysteines in proteins has hindered their discovery and characterization. Here we

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