909599
DHSO crosslinker
동의어(들):
3,3′-Sulfinyldi(propanehydrazide), Dihydrazide sulfoxide, Mass spectrometry-cleavable crosslinker for studying protein-protein interations
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About This Item
실험식(Hill 표기법):
C6H14N4O3S
CAS Number:
Molecular Weight:
222.27
MDL number:
UNSPSC 코드:
12161502
NACRES:
NA.22
추천 제품
양식
powder
저장 온도
2-8°C
SMILES string
[S](=O)(CCC(=O)NN)CCC(=O)NN
InChI key
XTCXQISMAWBOOT-UHFFFAOYSA-N
애플리케이션
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.
기타 정보
Technology Spotlight: Cross-Linkers for Elucidation of Protein-Protein Interactions
Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein–Protein Interactions
Development of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein–Protein Interactions
Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling
Developing an Acidic Residue Reactive and Sulfoxide-Containing MS-Cleavable Homobifunctional Cross-Linker for Probing Protein–Protein Interactions
Development of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein–Protein Interactions
Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling
법적 정보
Subject to US Patent Application #15/613,065 of the Regents of the University of California
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
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
문서
Sulfoxide-containing MS-cleavable cross-linkers capture protein-protein interactions in native cellular environments, aiding PPI identification.
Choosing the right crosslinker for your biochemical or bioconjugation research can be challenging. Our selection guide can help you find the perfect match for your applications.
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