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909602

Sigma-Aldrich

DSSO crosslinker

≥95%

Sinónimos:

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 (notación de Hill):
C14H16N2O9S
Número de CAS:
1351828-03-9
Peso molecular:
388.35
Número MDL:
MFCD30497419
Código UNSPSC:
12161502

Análisis

≥95%

formulario

powder

disponibilidad

available only in USA

temp. de almacenamiento

2-8°C

Aplicación

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.

Otras notas

Technology Spotlight: Cross-Linkers for Elucidation of Protein-Protein Interactions

Development of a novel cross-linking strategy for fast and accurate identification of cross-linked peptides of protein complexes

Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling

Developing a Multiplexed Quantitative Cross-Linking Mass Spectrometry Platform for Comparative Structural Analysis of Protein Complexes

Development of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein–Protein Interactions

Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein-Protein Interactions

Información legal

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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Pictogramas

Flame
GHS02

Palabra de señalización

Danger

Frases de peligro

H242

Clasificaciones de peligro

Self-react. C

Código de clase de almacenamiento

5.2 - Organic peroxides and self-reacting hazardous materials

Clase de riesgo para el agua (WGK)

WGK 3

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Certificados de análisis (COA)

Lot/Batch Number

Lo sentimos, en este momento no disponemos de COAs para este producto en línea.

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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

Artículos

Sulfoxide-Containing Mass Spectrometry (MS)-Cleavable Cross-Linkers

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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