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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
MDL number:
MFCD30497419
UNSPSC Code:
12161502

assay

≥95%

form

powder

availability

available only in USA

storage temp.

2-8°C

SMILES string

[S](=O)(CCC(=O)ON2C(=O)CCC2=O)CCC(=O)ON1C(=O)CCC1=O

InChI key

XJSVVHDQSGMHAJ-UHFFFAOYSA-N

Application

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.

Other Notes

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

Legal Information

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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909629

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909599

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909661

d0-DMDSSO crosslinker, ≥95%

909688

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pictograms

Flame
GHS02

signalword

Danger

hcodes

H242

Hazard Classifications

Self-react. C

Storage Class

5.2 - Organic peroxides and self-reacting hazardous materials

wgk_germany

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

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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