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909629

Sigma-Aldrich

Azide-A-DSBSO crosslinker

≥95%

Synonym(s):

Azide-tagged acid-cleavable disuccinimidyl bissulfoxide, Bis(2,5-dioxopyrrolidin-1-yl) 3,3′-((2-(3-azidopropyl)-2-methyl-1,3-dioxane-5,5-diyl)bis(methylenesulfinyl))dipropionate, Mass spectrometry-cleavable crosslinker for studying protein-protein interations

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About This Item

Empirical Formula (Hill Notation):
C24H33N5O12S2
CAS Number:
Molecular Weight:
647.68
UNSPSC Code:
12161502

Quality Level

Assay

≥95%

form

powder

availability

available only in USA

storage temp.

2-8°C

Application

Azide-A-DSBSO (azide-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).
Azide-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 azide tag permits selective enrichment of crosslinked proteins or peptides with a biotin-conjugated alkyne probe to enhance their detection. Additionally, the post-cleavage spacer yields tagged peptides for unambiguous identification by collision-induced dissociation in tandem MS.
Azide-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.

Legal Information

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

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Storage Class Code

4.1B - Flammable solid hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Robyn M Kaake et al.
Molecular & cellular proteomics : MCP, 13(12), 3533-3543 (2014-09-26)
Protein-protein interactions (PPIs) are fundamental to the structure and function of protein complexes. Resolving the physical contacts between proteins as they occur in cells is critical to uncovering the molecular details underlying various cellular activities. To advance the study of
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

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