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Key Documents

909602

Sigma-Aldrich

DSSO crosslinker

≥95%

Sinônimo(s):

Bis(2,5-dioxopyrrolidin-1-yl) 3,3′-sulfinyldipropionate, Bis-(propionic acid NHS ester)-sulfoxide, Mass spectrometry-cleavable crosslinker for studying protein-protein interations

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About This Item

Fórmula empírica (Notação de Hill):
C14H16N2O9S
Número CAS:
Peso molecular:
388.35
Número MDL:
Código UNSPSC:
12161502

Ensaio

≥95%

forma

powder

disponibilidade

available only in USA

temperatura de armazenamento

2-8°C

Aplicação

DSSO (disuccinimidyl sulfoxide) crosslinker is a homobifunctional, amine-targeting, sulfoxide-containing crosslinker for analysis of protein-protein interactions (PPIs) through crosslinking mass spectrometry (XL-MS). Membrane-permeable DSSO possesses two N-hydroxysuccinimide (NHS) esters for targeting Lys, a 10.1 Å spacer arm, and two symmetrical C-S cleavable bonds adjacent to the central sulfoxide. The post-cleavage spacer yields tagged peptides for unambiguous identification by collision-induced dissociation in tandem MS. DSSO Crosslinker provides complementary data to thiol-reactive and acidic residue-targeting reagents and will find wide utility in the elucidation of PPIs, study of proteins that function as complexes, quantification of structural dynamics, and the quest for targeting ″undruggable″ protein targets.

Informações legais

Subject to US Patent #9,222,943 and US Patent Application #15/275,001 of the Regents of the University of California

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Frases de perigo

Classificações de perigo

Self-react. C

Código de classe de armazenamento

5.2 - Organic peroxides and self-reacting hazardous materials

Classe de risco de água (WGK)

WGK 3


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Christian E Stieger et al.
Journal of proteome research, 18(3), 1363-1370 (2019-01-30)
Cross-linking mass spectrometry is becoming increasingly popular, and current advances are widening the applicability of the technique so that it can be utilized by nonspecialist laboratories. Specifically, the use of novel mass-spectrometry-cleavable (MS-cleavable) reagents dramatically reduces the complexity of the
Tara K Bartolec et al.
Analytical chemistry, 92(2), 1874-1882 (2019-12-19)
Saccharomyces cerevisiae has the most comprehensively characterized protein-protein interaction network, or interactome, of any eukaryote. This has predominantly been generated through multiple, systematic studies of protein-protein interactions by two-hybrid techniques and of affinity-purified protein complexes. A pressing question is to
Clinton Yu et al.
Analytical chemistry, 88(20), 10301-10308 (2016-10-19)
Cross-linking mass spectrometry (XL-MS) represents a recently popularized hybrid methodology for defining protein-protein interactions (PPIs) and analyzing structures of large protein assemblies. In particular, XL-MS strategies have been demonstrated to be effective in elucidating molecular details of PPIs at the

Artigos

Learn about homobifunctional sulfoxide-containing MS-cleavable cross-linkers that enables the capture of protein-protein interactions (PPIs) in native cellular environments, and the identification of cross-linked peptides permits the determination of both identity and connectivity of PPIs.

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