Alle Fotos(2)
Wichtige Dokumente
909602
DSSO crosslinker
≥95%
Synonym(e):
Bis(2,5-dioxopyrrolidin-1-yl) 3,3′-sulfinyldipropionate, Bis-(propionic acid NHS ester)-sulfoxide, Mass spectrometry-cleavable crosslinker for studying protein-protein interations
Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Alle Fotos(2)
About This Item
Empirische Formel (Hill-System):
C14H16N2O9S
CAS-Nummer:
Molekulargewicht:
388.35
MDL-Nummer:
UNSPSC-Code:
12161502
Preise und Verfügbarkeit sind derzeit nicht verfügbar.
Empfohlene Produkte
Assay
≥95%
Form
powder
Verfügbarkeit
available only in USA
Lagertemp.
2-8°C
SMILES String
[S](=O)(CCC(=O)ON2C(=O)CCC2=O)CCC(=O)ON1C(=O)CCC1=O
InChIKey
XJSVVHDQSGMHAJ-UHFFFAOYSA-N
Anwendung
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.
Sonstige Hinweise
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
Rechtliche Hinweise
Subject to US Patent #9,222,943 and US Patent Application #15/275,001 of the Regents of the University of California
Ähnliches Produkt
Signalwort
Danger
H-Sätze
Gefahreneinstufungen
Self-react. C
Lagerklassenschlüssel
5.2 - Organic peroxides and self-reacting hazardous materials
WGK
WGK 3
Hier finden Sie alle aktuellen Versionen:
Analysenzertifikate (COA)
Lot/Batch Number
Die passende Version wird nicht angezeigt?
Wenn Sie eine bestimmte Version benötigen, können Sie anhand der Lot- oder Chargennummer nach einem spezifischen Zertifikat suchen.
Besitzen Sie dieses Produkt bereits?
In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.
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
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
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
Artikel
Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.
Active Filters
Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..
Setzen Sie sich mit dem technischen Dienst in Verbindung.
