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DHSO crosslinker

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3,3′-Sulfinyldi(propanehydrazide), Dihydrazide sulfoxide, Mass spectrometry-cleavable crosslinker for studying protein-protein interations
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DHSO crosslinker



DHSO crosslinker

DSSO crosslinker ≥95%



DSSO crosslinker

storage temp.


storage temp.


storage temp.


storage temp.



DHSO Crosslinker is a homobifunctional, acidic residue-targeting, sulfoxide-containing crosslinker for analysis of protein-protein interactions (PPIs) through crosslinking mass spectrometry (XL-MS). DHSO possesses two hydrazide-reactive groups for targeting aspartic acid (Asp) and glutamic acid (Glu) and two symmetrical C-S cleavable bonds adjacent to the central sulfoxide. While former amine-reactive reagents react with lysine (Lys) residues in proximity to the PPI, targeting acidic residues provides further opportunity to characterize protein interaction surfaces at which Asp and Glu are often prevalent. Additionally, the 12.4 Å spacer yields tagged peptides post-cleavage for unambiguous identification by collision-induced dissociation in tandem MS. DHSO Crosslinker provides complementary data to Lys-targeting reagents and will find wide utility in the elucidation of PPIs, study of proteins that function as complexes, quantification of structural dynamics, and quest for targeting "undruggable" protein targets.

Legal Information

Subject to US Patent Application #15/613,065 of the Regents of the University of California

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Storage Class Code

11 - Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Craig B Gutierrez et al.
Analytical chemistry, 88(16), 8315-8322 (2016-07-16)
Cross-linking mass spectrometry (XL-MS) has become a powerful strategy for defining protein-protein interactions and elucidating architectures of large protein complexes. However, one of the inherent challenges in MS analysis of cross-linked peptides is their unambiguous identification. To facilitate this process
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


Sulfoxide-Containing Mass Spectrometry (MS)-Cleavable Cross-Linkers

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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