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A1632

Sigma-Aldrich

DL-7-Azatryptophan hydrate

≥98% (TLC)

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About This Item

Empirical Formula (Hill Notation):
C10H11N3O2 · H2O
CAS Number:
Molecular Weight:
223.23
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26

Product Name

DL-7-Azatryptophan hydrate,

Assay

≥98% (TLC)

form

powder

color

white to off-white

storage temp.

−20°C

SMILES string

O.NC(Cc1c[nH]c2ncccc12)C(O)=O

InChI

1S/C10H11N3O2.H2O/c11-8(10(14)15)4-6-5-13-9-7(6)2-1-3-12-9;/h1-3,5,8H,4,11H2,(H,12,13)(H,14,15);1H2

InChI key

PXDRHYQAIUZKHN-UHFFFAOYSA-N

Biochem/physiol Actions

DL-7-Azatryptophan is a racemic mixture of D- and L-7-azatryptophan which together with L-tryptophan is a synergistic inducer of tryptophan oxygenase of Pseudomonas acidovorans. DL-7-Azatryptophan inhibits photosynthetic carbon assimilation, photosynthetic oxygen evolution and nitrogen metabolism in Anabaena sp. Strain 1F, a marine filamentous, heterocystous cyanobacterium.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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J Guharay et al.
Biochemical and biophysical research communications, 219(2), 388-392 (1996-02-15)
The amino acid analogue 7-azatryptophan has attracted significant recent attention as a novel optical probe for protein structure, function and dynamics. We report here, for the first time, its fluorescence emission behavior in a membrane mimetic model system, namely reverse
Michael Georg Hoesl et al.
Journal of peptide science : an official publication of the European Peptide Society, 16(10), 589-595 (2010-07-16)
Aequorea victoria green fluorescent protein and its widely used mutants enhanced green fluorescent protein and enhanced cyan fluorescent protein (ECFP) are ideal target proteins to study protein folding. The spectral signals of their chromophores are directly correlated with the folding
Lars Merkel et al.
Chembiochem : a European journal of chemical biology, 11(3), 305-314 (2010-01-09)
In vivo expression of colored proteins without post-translational modification or chemical functionalization is highly desired for protein studies and cell biology. Cell-permeable tryptophan analogues, such as azatryptophans, have proved to be almost ideal isosteric substitutes for natural tryptophan in cellular
C W Hogue et al.
Biophysical chemistry, 48(2), 159-169 (1993-12-01)
The tryptophan analogs 5-hydroxytryptophan (5HW) and 7-azatryptophan (7AW) are capable of being biosynthetically incorporated into bacterial proteins and can be used as intrinsic fluorescence probes of protein structure, function and dynamics. A prerequisite for analog incorporation is their recognition by
C Y Wong et al.
Protein science : a publication of the Protein Society, 6(3), 689-697 (1997-03-01)
5-Hydroxytryptophan (5HW) and 7-azatryptophan (7AW) are analogue of tryptophan that potentially can be incorporated biosynthetically into proteins and used as spectroscopic probes for studying protein-DNA and protein-protein complexes. The utility of these probes will depend on the extent to which

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