927600
BrBT-alkyne
≥95%
别名:
2-Bromo-N-(prop-2-yn-1-yl)benzo[d]thiazole-6-carboxamide
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关于此项目
经验公式（希尔记法）:
C11H7BrN2OS
化学文摘社编号:
分子量:
295.16
MDL number:
UNSPSC Code:
12352101
NACRES:
NA.22
产品名称
BrBT-alkyne, ≥95%
InChI
1S/C11H7BrN2OS/c1-2-5-13-10(15)7-3-4-8-9(6-7)16-11(12)14-8/h1,3-4,6H,5H2,(H,13,15)
InChI key
MRYSQSUDZPBHGP-UHFFFAOYSA-N
SMILES string
BrC1=NC2=CC=C(C(NCC#C)=O)C=C2S1
assay
≥95%
form
powder
storage temp.
−20°C
Quality Level
Application
BrBT-alkyne is a probe that can be used to lable cysteines through nucleophilic aromatic substitution. A method was developed using cysteine-reactive compounds including this one to allow for unbiased analysis of proteomic data in quantitave applications (Zanon et al. 2021). The method uses light or heavy labeling with the isotopically labelled desthiobiotin azide (isoDTB) tag for mass spectrometry analysis (Zanon et al. 2020). Analysis then uses the isotopic tandem orthogonal proteolysis activity-based protein profiling (isoTOP-ABPP) workflow (Weerapana et al. 2010, Backus et al. 2016).
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Profiling the proteome-wide selectivity of diverse electrophiles.
Zanon P RA, et al
ChemRxiv : the preprint server for chemistry (2021)
Isotopically Labeled Desthiobiotin Azide (isoDTB) Tags Enable Global Profiling of the Bacterial Cysteinome.
Zanon P R A, et al.
Angewandte Chemie (International Edition in English), 2829-2836 (2020)
Patrick R A Zanon et al.
Angewandte Chemie (International ed. in English), 59(7), 2829-2836 (2019-11-30)
Rapid development of bacterial resistance has led to an urgent need to find new druggable targets for antibiotics. In this context, residue-specific chemoproteomic approaches enable proteome-wide identification of binding sites for covalent inhibitors. Described here are easily synthesized isotopically labeled
Eranthie Weerapana et al.
Nature, 468(7325), 790-795 (2010-11-19)
Cysteine is the most intrinsically nucleophilic amino acid in proteins, where its reactivity is tuned to perform diverse biochemical functions. The absence of a consensus sequence that defines functional cysteines in proteins has hindered their discovery and characterization. Here we
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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