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N3253

Sigma-Aldrich

2-Nitrophenyl β-D-fucopyranoside

≥99% (TLC)

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About This Item

Empirische Formel (Hill-System):
C12H15NO7
CAS-Nummer:
1154-94-5
Molekulargewicht:
285.25
MDL-Nummer:
MFCD00057511
UNSPSC-Code:
12352204
PubChem Substanz-ID:
24897632

Assay

≥99% (TLC)

Lagertemp.

−20°C

SMILES String

CC1OC(Oc2ccccc2N(=O)=O)C(O)C(O)C1O

InChI

1S/C12H15NO7/c1-6-9(14)10(15)11(16)12(19-6)20-8-5-3-2-4-7(8)13(17)18/h2-6,9-12,14-16H,1H3

InChIKey

SWRPIVXPHLYETN-UHFFFAOYSA-N

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Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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C E Bell et al.
Nature structural biology, 7(3), 209-214 (2000-03-04)
Crystal structures of the Lac repressor, with and without isopropyithiogalactoside (IPTG), and the repressor bound to operator have provided a model for how the binding of the inducer reduces the affinity of the repressor for the operator. However, because of
S P Manly et al.
Biochemistry, 24(15), 3842-3846 (1985-07-16)
The thermal denaturation of the core protein of lac repressor was studied alone and in the presence of the inducer isopropyl beta-D-thiogalactoside (IPTG) and the antiinducer o-nitrophenyl beta-D-fucoside (ONPF) by means of high-sensitivity differential scanning calorimetry. The denaturation that takes
Corey J Wilson et al.
Biophysical chemistry, 126(1-3), 94-105 (2006-07-25)
Specific interactions between proteins and ligands that modify their functions are crucial in biology. Here, we examine sugars that bind the lactose repressor protein (LacI) and modify repressor affinity for operator DNA using isothermal titration calorimetry and equilibrium DNA binding
N Horton et al.
Journal of molecular biology, 265(1), 1-7 (1997-01-10)
The wild type E. coli lac operator is embedded in a 35 base-pair DNA sequence containing extensive 2-fold symmetry, suggesting a symmetric repressor operator complex. However, deviations from strict 2-fold symmetry occur at the central base-pair and at three additional
Liskin Swint-Kruse
Biochemistry, 43(34), 10886-10895 (2004-08-25)
The vast increase in available data from the "-omics" revolution has enabled the fields of structural proteomics and structure prediction to make great progress in assigning realistic three-dimensional structures to each protein molecule. The challenge now lies in determining the
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