792551
H-4-(7-Hydroxy-4-coumarinyl)-Abu-OH
98% (HPLC)
Synonyme(s) :
(S)-2-Amino-4-(7-hydroxy-2-oxo-2H-chromen-4-yl)butanoic acid, Schultz Fluorescent UAA
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About This Item
Produits recommandés
Pureté
98% (HPLC)
Forme
solid
Activité optique
[α]22/D +8.0°, c = 0.5% in 1 M NaOH
Pf
276-281 °C
Température de stockage
15-25°C
Application
The courmarin-based unnatural amino acid is an effective fluorophore; which has been incoporated into several studies of protein interactions.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Journal of the American Chemical Society, 133(38), 14936-14939 (2011-08-30)
As newly synthesized proteins emerge from the ribosome, they interact with a variety of cotranslational cellular machineries that facilitate their proper folding, maturation, and localization. These interactions are essential for proper function of the cell, and the ability to study
Bioorganic & medicinal chemistry letters, 21(24), 7502-7504 (2011-11-02)
The site-specific incorporation of unnatural amino acids (UAAs) into proteins in bacteria is made possible by the evolution of aminoacyl-tRNA synthetases that selectively recognize and aminoacylate the amino acid of interest. Recently we have discovered that some of the previously
Journal of the American Chemical Society, 128(27), 8738-8739 (2006-07-06)
The fluorescent amino acid l-(7-hydroxycoumarin-4-yl) ethylglycine 1 has been genetically encoded in E. coli in response to the amber TAG codon. Because of its high fluorescence quantum yield, relatively large Stoke's shift, and sensitivity to both pH and polarity, this
Bioorganic & medicinal chemistry, 21(2), 553-559 (2012-12-15)
Incorporation of the unnatural amino acid L-(7-hydroxycoumarin-4-yl)ethylglycine (7-HC) is a powerful and reliable approach for the preparation of fluorescently labeled proteins. The growing popularity of this valuable amino acid prompted us to pursue an improved protocol for its synthetic preparation.
Journal of the American Chemical Society, 135(35), 12924-12927 (2013-08-15)
Two fluorescent amino acids, including the novel fluorescent species 4-biphenyl-l-phenylalanine (1), have been incorporated at positions 17 and 115 of dihydrofolate reductase (DHFR) to enable a study of conformational changes associated with inhibitor binding. Unlike most studies involving fluorescently labeled
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
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