Alkyne-A-DSBSO crosslinker


Alkyne-tagged acid-cleavable disuccinimidyl bissulfoxide, Mass spectrometry-cleavable crosslinker for studying protein-protein interactions, Bis(2,5-dioxopyrrolidin-1-yl) 3,3′-((2-(but-3-yn-1-yl)-2-methyl-1,3-dioxane-5,5-diyl)bis(methylenesulfinyl))dipropionate
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available only in USA

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Alkyne-A-DSBSO (alkyne-tagged, acid-cleavable disuccinimidyl bissulfoxide) Crosslinker is a homobifunctional, membrane-permeable, enrichable disulfoxide-containing crosslinker for analysis of protein-protein interactions (PPIs) through crosslinking mass spectrometry (XL-MS).
Alkyne-A-DSBSO possesses two N-hydroxysuccinimide (NHS) ester groups for targeting amines, a ∼14 Å spacer length, two symmetrical acid-cleavable C-S bonds, and a central bioorthogonal azide tag. After reacting with lysine (Lys) residues, the alkyne tag permits selective enrichment of crosslinked proteins or peptides with a biotin-conjugated azide probe to enhance their detection. Additionally, the post-cleavage spacer yields tagged peptides for unambiguous identification by collision-induced dissociation in tandem MS.
Alkyne-A-DSBSO Crosslinker has mapped in vivo PPIs for target protein complexes and whole proteomes from living cells. It will also be a useful proteomics tool in the quest for targeting ″undruggable″ protein targets.

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Subject to US Patent Application #15/275,001 of the Regents of the University of California



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Certificate of Analysis
Certificate of Origin
Anthony M Burke et al.
Organic & biomolecular chemistry, 13(17), 5030-5037 (2015-04-01)
The cross-linking Mass Spectrometry (XL-MS) technique extracts structural information from protein complexes without requiring highly purified samples, crystallinity, or large amounts of material. However, there are challenges to applying the technique to protein complexes in vitro, and those challenges become...
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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