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Merck
CN

925144

Sigma-Aldrich

KB05yne

≥95%

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别名:
4-(N-(4-Bromophenyl)acrylamido)-N-(hex-5-yn-1-yl)benzamide, Functionalized scout fragment
经验公式(希尔记法):
C22H21BrN2O2
分子量:
425.32
UNSPSC代码:
12352101
NACRES:
NA.22

质量水平

检测方案

≥95%

形式

powder or solid

反应适用性

reagent type: chemical modification reagent
reaction type: click chemistry

储存温度

2-8°C

应用

KB05yne 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), KB02yne (925225) Electrophilic 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)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), KB02yne (925225) Electrophilic 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

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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Electrophilic PROTACs that degrade nuclear proteins by engaging DCAF16
Xiaoyu Zhang, et al
Nature Chemical Biology, 15(7), 737-746 (2019)
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
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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