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Merck

925225

Sigma-Aldrich

KB02yne

Sinónimos:

2-Chloro-1-(6-(hex-5-yn-1-yloxy)-3,4-dihydroquinolin-1(2H)-yl)ethan-1-one, Functionalized scout fragment

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About This Item

Fórmula empírica (notación de Hill):
C17H20ClNO2
Número de CAS:
Peso molecular:
305.80
UNSPSC Code:
12352101
NACRES:
NA.22

form

powder or crystals (or Solid or Liquid)

Quality Level

reaction suitability

reagent type: chemical modification reagent
reaction type: click chemistry

storage temp.

2-8°C

Categorías relacionadas

Application

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

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Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3


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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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