927546
CA-nitrile
≥95%
Sinônimo(s):
2-Chloro-N-(4-cyanobutyl)acetamide
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About This Item
Fórmula empírica (Notação de Hill):
C7H11ClN2O
Número CAS:
Peso molecular:
174.63
Número MDL:
Código UNSPSC:
12352101
NACRES:
NA.21
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Nível de qualidade
Ensaio
≥95%
Formulário
viscous liquid
temperatura de armazenamento
−20°C
cadeia de caracteres SMILES
O=C(NCCCCC#N)CCl
InChI
1S/C7H11ClN2O/c8-6-7(11)10-5-3-1-2-4-9/h1-3,5-6H2,(H,10,11)
chave InChI
ZZLJGFMMZIPIAF-UHFFFAOYSA-N
Aplicação
CA-nitrile is a negative control probe that can be used for labeling cysteines through alkylation but lacks an alkyne necessary for labeling. 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).
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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Certificados de análise (COA)
Lot/Batch Number
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Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
Isotopically Labeled Desthiobiotin Azide (isoDTB) Tags Enable Global Profiling of the Bacterial Cysteinome.
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
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