925225
KB02yne
别名:
2-Chloro-1-(6-(hex-5-yn-1-yloxy)-3,4-dihydroquinolin-1(2H)-yl)ethan-1-one, Functionalized scout fragment
表单
powder or crystals (or Solid or Liquid)
质量水平
反应适用性
reagent type: chemical modification reagent
reaction type: click chemistry
储存温度
2-8°C
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:
Technology spotlight: Proteomic Ligandability Assessment
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
储存分类代码
10 - Combustible liquids
WGK
WGK 3
法规信息
新产品
此项目有
历史批次信息供参考:
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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