F7376
4-Fluoro-DL-tryptophan
crystalline
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About This Item
Formule empirique (notation de Hill) :
C11H11FN2O2
Numéro CAS:
Poids moléculaire :
222.22
Numéro MDL:
Code UNSPSC :
12352200
ID de substance PubChem :
Nomenclature NACRES :
NA.26
Produits recommandés
Essai
≥98.0% (TLC)
Forme
crystalline
Technique(s)
NMR: suitable
Couleur
off-white
Température de stockage
−20°C
Chaîne SMILES
NC(Cc1c[nH]c2cccc(F)c12)C(O)=O
InChI
1S/C11H11FN2O2/c12-7-2-1-3-9-10(7)6(5-14-9)4-8(13)11(15)16/h1-3,5,8,14H,4,13H2,(H,15,16)
Clé InChI
DEBQMEYEKKWIKC-UHFFFAOYSA-N
Actions biochimiques/physiologiques
4-Fluoro-DL-tryptophan (4-F-TRP) is used to label bacterial arginyl-tRNA synthetases for conformational analysis and to label myoglobins and hemoglobins for NMR spectra analysis.
Code de la classe de stockage
13 - Non 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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P Soumillion et al.
Biochemistry, 37(7), 1819-1827 (1998-03-04)
Clamp proteins confer processivity to the DNA polymerase during DNA replication. These oligomeric proteins are loaded onto DNA by clamp loader protein complexes in an ATP-dependent manner. The mechanism by which the trimeric bacteriophage T4 clamp protein (the 45 protein)
P M Bronskill et al.
The Biochemical journal, 249(1), 305-308 (1988-01-01)
The tryptophan-auxotrophic Bacillus subtilis LC33 mutant strain utilizes either tryptophan or 4-fluorotryptophan for growth. Proteins therefore could be isolated from these cells in either tryptophan-containing or 4-fluorotryptophan-containing forms. Since 4-fluorotryptophan is non-fluorescent, tryptophan fluorescence would be suppressed in the 4-fluorotryptophan-containing
Q S Zhang et al.
Journal of protein chemistry, 18(2), 187-192 (1999-05-20)
Escherichia coli 4-fluorotryptophan-substituted arginyl-tRNA synthetase was biosynthetically prepared and purified from a tryptophan auxotroph which could overproduce this enzyme. A method was developed to separate 4-fluorotryptophan from tryptophan and to determine accurately their contents in the 4-fluorotryptophan-containing proteins. It was
J G Pearson et al.
Biochemistry, 36(12), 3590-3599 (1997-03-25)
We have obtained the 470 MHz 19F NMR spectra of wild type [4-F]Trp-labeled myoglobins (MbCO, MbO2, deoxyMb, metMb, and MbCN) and hemoglobins (HbCO, HbO2, and deoxyHb), as well as those of several mutants (W7F Mb, betaW15F Hb, betaW37S Hb, and
Yong-Neng Yao et al.
FEBS letters, 547(1-3), 197-200 (2003-07-16)
The 19F nuclear magnetic resonance (NMR) spectra of 4-fluorotryptophan (4-F-Trp)-labeled Escherichia coli arginyl-tRNA synthetase (ArgRS) show that there are distinct conformational changes in the catalytic core and tRNA anticodon stem and loop-binding domain of the enzyme, when arginine and tRNA(Arg)
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