909602
DSSO crosslinker
≥95%
Synonyme(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
Formule empirique (notation de Hill):
C14H16N2O9S
Numéro CAS:
Poids moléculaire :
388.35
Numéro MDL:
Code UNSPSC :
12161502
Produits recommandés
Pureté
≥95%
Forme
powder
Disponibilité
available only in USA
Température de stockage
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.
Autres remarques
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
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
Informations légales
Subject to US Patent #9,222,943 and US Patent Application #15/275,001 of the Regents of the University of California
Produit(s) apparenté(s)
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Self-react. C
Code de la classe de stockage
5.2 - Organic peroxides and self-reacting hazardous materials
Classe de danger pour l'eau (WGK)
WGK 3
Certificats d'analyse (COA)
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
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
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
Athit Kao et al.
Molecular & cellular proteomics : MCP, 10(1), M110-M110 (2010-08-26)
Knowledge of elaborate structures of protein complexes is fundamental for understanding their functions and regulations. Although cross-linking coupled with mass spectrometry (MS) has been presented as a feasible strategy for structural elucidation of large multisubunit protein complexes, this method has
Lei Lu et al.
Journal of proteome research, 17(7), 2370-2376 (2018-05-26)
Protein chemical cross-linking combined with mass spectrometry has become an important technique for the analysis of protein structure and protein-protein interactions. A variety of cross-linkers are well developed, but reliable, rapid, and user-friendly tools for large-scale analysis of cross-linked proteins
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
Articles
Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.
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