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909602

Sigma-Aldrich

DSSO crosslinker

≥95%

Synonym(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

Empirical Formula (Hill Notation):
C14H16N2O9S
CAS Number:
1351828-03-9
Molecular Weight:
388.35
MDL number:
MFCD30497419
UNSPSC Code:
12161502

Assay

≥95%

form

powder

availability

available only in USA

storage temp.

2-8°C

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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Description
Pricing

Pictograms

Flame
GHS02

Signal Word

Danger

Hazard Statements

H242

Hazard Classifications

Self-react. C

Storage Class Code

5.2 - Organic peroxides and self-reacting hazardous materials

WGK

WGK 3

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Certificates of Analysis (COA)

Lot/Batch Number
MKCV8088
MKCS6678

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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
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
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
Daniela-Lee Smith et al.
Analytical chemistry, 90(15), 9101-9108 (2018-07-14)
This study investigated the enzyme-substrate interaction between Saccharomyces cerevisiae arginine methyltransferase Hmt1p and nucleolar protein Npl3p, using chemical cross linking/mass spectrometry (XL/MS). We show that XL/MS can capture transient interprotein interactions that occur during the process of methylation, involving a
Sebastiaan C de Graaf et al.
Journal of proteome research, 18(2), 642-651 (2018-12-24)
Protein interactions enable much more complex behavior than the sum of the individual protein parts would suggest and represents a level of biological complexity requiring full understanding when unravelling cellular processes. Cross-linking mass spectrometry has emerged as an attractive approach
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Articles

MS-Cleavable Cross-Linkers

Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.

MS-Cleavable Cross-Linkers

Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.

MS-Cleavable Cross-Linkers

Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.

MS-Cleavable Cross-Linkers

Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.

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