Merck
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安全信息

925225

Sigma-Aldrich

KB02yne

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别名:
2-Chloro-1-(6-(hex-5-yn-1-yloxy)-3,4-dihydroquinolin-1(2H)-yl)ethan-1-one, Functionalized scout fragment
经验公式（希尔记法）:
C17H20ClNO2
CAS号:
2376152-06-4
分子量:
305.80

形式

powder or crystals (or Solid or Liquid)

质量水平

100

反应适用性

reagent type: chemical modification reagent
reaction type: click chemistry

储存温度

2-8°C

相关类别

应用

KB02yne 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 is the functionalized version of KB02 (912131).

Related useful products may include:
  • Cysteine-reactive fragments: KB02 (912131), KB03 (912654), KB05 (911798), sulfoxide (925136), CoLDR probe (923818)
  • Functionalized scout fragments: KB02-COOH (925047), KB05yne (925144)
  • Electrophilc degraders featuring scout fragments: KB02-SLF (914738), KB03-SLF (914975), KB05-SLF (913715), Biotin-SLF (914223)
  • Cysteine-reactive probes for chemoproteomics: IA alkyne (924237), IA 5-TAMRA (925020), desthiobiotin iodoacetamide (923826), or biotin iodoacetamide (B2059)

Technology spotlight: Proteomic Ligandability Assessment

其他说明

Functionalized Scout Fragments for Site-Specific Covalent Ligand Discovery and Optimization

The Proteome-Wide Potential for Reversible Covalency at Cysteine

Electrophilic PROTACs that degrade nuclear proteins by engaging DCAF16

储存分类代码

10 - Combustible liquids

WGK

WGK 3

法规信息

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Vincent M Crowley et al.
ACS central science, 7(4), 613-623 (2021-06-01)
Covalent ligands are a versatile class of chemical probes and drugs that can target noncanonical sites on proteins and display differentiated pharmacodynamic properties. Chemical proteomic methods have been introduced that leverage electrophilic fragments to globally profile the covalent ligandability of
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

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