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Merck

909610

Sigma-Aldrich

BMSO crosslinker

≥95%

别名:

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

经验公式(希尔记法):
C18H22N4O7S
分子量:
438.45
分類程式碼代碼:
12352200
NACRES:
NA.22

化驗

≥95%

形狀

powder

儲存溫度

2-8°C

應用

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.

法律資訊

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

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产品编号
说明
价格

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°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

商品

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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