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A1632

Sigma-Aldrich

DL-7-Azatryptophan hydrate

≥98% (TLC)

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About This Item

Fórmula empírica (Notação de Hill):
C10H11N3O2 · H2O
Número CAS:
7146-37-4
Peso molecular:
223.23
Número MDL:
MFCD00150525
Código UNSPSC:
12352209
ID de substância PubChem:
24890571
NACRES:
NA.26

product name

DL-7-Azatryptophan hydrate,

Ensaio

≥98% (TLC)

forma

powder

cor

white to off-white

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

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

chave InChI

PXDRHYQAIUZKHN-UHFFFAOYSA-N

Ações bioquímicas/fisiológicas

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.

Aplicação

Nº do produto
Descrição
Preços

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificados de análise (COA)

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Julie M G Rogers et al.
Analytical biochemistry, 399(2), 182-189 (2009-12-29)
Fluorescence resonance energy transfer (FRET) provides a powerful means to study protein conformational changes. However, the incorporation of an exogenous FRET pair into a protein could lead to undesirable structural perturbations of the native fold. One of the viable strategies
Arnaldo L Serrano et al.
The journal of physical chemistry. B, 116(35), 10631-10638 (2012-08-16)
The villin headpiece subdomain (HP35) has become one of the most widely used model systems in protein folding studies, due to its small size and ultrafast folding kinetics. Here, we use HP35 as a test bed to show that the
P Soumillion et al.
Protein engineering, 8(5), 451-456 (1995-05-01)
The phage lambda lysozyme (lambda L) contains four tryptophans. These have been efficiently replaced by 7-azatryptophan (7aW) through biosynthetic incorporation into the overexpressed protein. Comparative analysis of the effect of temperature or pH on the fluorescence of the wild-type lambda
Fernando Formaggio et al.
Advances in experimental medicine and biology, 527, 731-737 (2004-06-23)
Aal and 7-Atrp, quasi-isosteric with Trp, have been inserted together with a TOAC residue in two 3(10)-helical, model hexapeptides. The interaction of photoexcited AA1 and 7-Atrp with the nitroxide group of TOAC was investigated by time resolved EPR. Both peptides
Vasant Muralidharan et al.
Journal of the American Chemical Society, 126(43), 14004-14012 (2004-10-28)
An integrated approach is described that allows the domain-specific incorporation of optical probes into large recombinant proteins. The strategy is the combination of two existing techniques, expressed protein ligation (EPL) and in vivo amino acid replacement of tryptophans with tryptophan
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Chromatograms

application for HPLC

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