912131
2-Chloro-1-(6-methoxy-1,2,3,4-tetrahydroquinolin-1-yl)ethan-1-one
≥95%
别名:
1-(Chloroacetyl)-1,2,3,4-tetrahydro-6-quinolinyl methyl ether, 2-Chloro-1-(6-methoxy-3,4-dihydroquinolin-1(2H)-yl)ethan-1-one, Electrophilic scout fragment, KB02, Scout fragment for targetable cysteine
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关于此项目
经验公式（希尔记法）:
C12H14ClNO2
化学文摘社编号:
分子量:
239.70
UNSPSC Code:
12352200
NACRES:
NA.22
MDL number:
产品名称
2-Chloro-1-(6-methoxy-1,2,3,4-tetrahydroquinolin-1-yl)ethan-1-one, ≥95%
SMILES string
ClCC(=O)N1CCCc2c1ccc(c2)OC
InChI
1S/C12H14ClNO2/c1-16-10-4-5-11-9(7-10)3-2-6-14(11)12(15)8-13/h4-5,7H,2-3,6,8H2,1H3
InChI key
XJPUWRWIBSSPSL-UHFFFAOYSA-N
assay
≥95%
form
chunks
storage temp.
2-8°C
Quality Level
Application
2-Chloro-1-(6-methoxy-1,2,3,4-tetrahydroquinolin-1-yl)ethan-1-one is a cysteine-reactive small-molecule fragment for chemoproteomic and ligandability studies for both traditionally druggable proteins as well as "undruggable," or difficult-to-target, proteins. This fragment electrophile, or "scout" fragment, can be used alone in fragment-based covalent ligand discovery or incorporated into bifunctional tools such as electrophilic PROTAC® molecules for targeted protein degradation as demonstrated by the Cravatt Lab Lab for E3 ligase discovery.
Other Notes
Legal Information
PROTAC is a registered trademark of Arvinas Operations, Inc., and is used under license
wgk
WGK 3
存储类别
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
Kristine Senkane et al.
Angewandte Chemie (International ed. in English), 58(33), 11385-11389 (2019-06-22)
Reversible covalency, achieved with, for instance, highly electron-deficient olefins, offers a compelling strategy to design chemical probes and drugs that benefit from the sustained target engagement afforded by irreversible compounds, while avoiding permanent protein modification. Reversible covalency has mainly been
Xiaoyu Zhang et al.
Nature chemical biology, 15(7), 737-746 (2019-06-19)
Ligand-dependent protein degradation has emerged as a compelling strategy to pharmacologically control the protein content of cells. So far, however, only a limited number of E3 ligases have been found to support this process. Here, we use a chemical proteomic
Keriann M Backus et al.
Nature, 534(7608), 570-574 (2016-06-17)
Small molecules are powerful tools for investigating protein function and can serve as leads for new therapeutics. Most human proteins, however, lack small-molecule ligands, and entire protein classes are considered 'undruggable'. Fragment-based ligand discovery can identify small-molecule probes for proteins
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