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Merck

912131

Sigma-Aldrich

2-Chloro-1-(6-methoxy-1,2,3,4-tetrahydroquinolin-1-yl)ethan-1-one

≥95%

Sinónimos:

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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About This Item

Fórmula empírica (notación de Hill):
C12H14ClNO2
Número de CAS:
Peso molecular:
239.70
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.22

Quality Level

assay

≥95%

form

chunks

storage temp.

2-8°C

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.

Legal Information

PROTAC is a registered trademark of Arvinas Operations, Inc., and is used under license

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Referencia del producto
Descripción
Precios

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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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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