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Merck

909610

Sigma-Aldrich

BMSO crosslinker

≥95%

Sinónimos:

3,3′-Sulfinylbis(N-(2-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)ethyl)propanamide), Mass spectrometry-cleavable crosslinker for studying protein-protein interations

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About This Item

Fórmula empírica (notación de Hill):
C18H22N4O7S
Número de CAS:
Peso molecular:
438.45
UNSPSC Code:
12352200
NACRES:
NA.22

assay

≥95%

form

powder

storage temp.

2-8°C

Application

BMSO (bismaleimide sulfoxide) crosslinker is a homobifunctional, cysteine residue-targeting, sulfoxide-containing crosslinker for analysis of protein-protein interactions (PPIs) through crosslinking mass spectrometry (XL-MS). BMSO possesses two maleimide reactive groups for targeting Cys, a 24.2 Å spacer arm, and two symmetrical C-S cleavable bonds adjacent to the central sulfoxide. While similar reagents react with lysine (Lys) and acidic residues, targeting Cys provides further opportunity to characterize protein interaction surfaces. Additionally, the post-cleavage spacer yields tagged peptides for unambiguous identification by collision-induced dissociation in tandem MS.

BMSO crosslinker provides complementary data to amine-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.

Legal Information

Subject to US provisional patent application #62/845,240 of the Regents of the University of California

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Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Craig B Gutierrez et al.
Analytical chemistry, 90(12), 7600-7607 (2018-05-25)
Cross-linking mass spectrometry (XL-MS) has become an emerging technology for defining protein-protein interactions (PPIs) and elucidating architectures of large protein complexes. Up to now, the most widely used cross-linking reagents target lysines. Although such reagents have been successfully applied to
Craig Gutierrez et al.
Proceedings of the National Academy of Sciences of the United States of America, 117(8), 4088-4098 (2020-02-09)
The COP9 signalosome (CSN) is an evolutionarily conserved eight-subunit (CSN1-8) protein complex that controls protein ubiquitination by deneddylating Cullin-RING E3 ligases (CRLs). The activation and function of CSN hinges on its structural dynamics, which has been challenging to decipher by

Artículos

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

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