307556
3,3,3-Trifluoro-DL-alanine
98%
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About This Item
Linear Formula:
CF3CH(NH2)CO2H
CAS Number:
Molecular Weight:
143.06
NACRES:
NA.22
PubChem Substance ID:
UNSPSC Code:
12352209
EC Number:
241-478-2
MDL number:
InChI key
HMJQKIDUCWWIBW-UHFFFAOYSA-N
InChI
1S/C3H4F3NO2/c4-3(5,6)1(7)2(8)9/h1H,7H2,(H,8,9)
SMILES string
NC(C(O)=O)C(F)(F)F
assay
98%
reaction suitability
reaction type: solution phase peptide synthesis
mp
231-234 °C (lit.)
application(s)
peptide synthesis
storage temp.
2-8°C
Quality Level
Storage Class
11 - Combustible Solids
wgk
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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T Clausen et al.
Journal of molecular biology, 262(2), 202-224 (1996-09-20)
Cystathionine beta-lyase (CBL) is a member of the gamma-family of PLP-dependent enzymes, that cleaves C beta-S bonds of a broad variety of substrates. The crystal structure of CBL from E. coli has been solved using MIR phases in combination with
Yong Guo et al.
Organic letters, 8(5), 827-829 (2006-02-24)
2-Aminoperfluoropropene has been prepared by the Mg-promoted defluorinative N-silylation of N-p-methoxyphenyl hexafluoroacetone imine and has been employed as a synthon of trifluoroalanine for the preparation of trifluoroalanine dipeptides.
L Pollegioni et al.
FEBS letters, 507(3), 323-326 (2001-11-07)
D-Amino acid oxidase (DAAO) is a flavoprotein oxidase that catalyzes the oxidation of amino acids and produces ketoacids and H(2)O(2). The rate of product release from reduced DAAO from Rhodotorula gracilis is pH dependent and reflects a pK(a) of approximately
E A Wang et al.
Biochemistry, 20(26), 7539-7546 (1981-12-22)
The alanine racemase from Escherichia coli B has been shown to process DL isomers of beta -fluoroalanine as suicide substrates with an identical partitioning ratio for each enantiomer of 820 catalytic eliminations of HF per enzymatic inactivation event [Wang, E.
R S Phillips et al.
Archives of biochemistry and biophysics, 296(2), 489-496 (1992-08-01)
Trifluoroalanine is a mechanism-based inactivator of Escherichia coli tryptophan indole-lyase (tryptophanase) and E. coli tryptophan synthase (R. B. Silverman and R. H. Abeles, 1976, Biochemistry 15, 4718-4723). We have found that indole is able to prevent inactivation of tryptophan indole-lyase
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