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About This Item
Empirical Formula (Hill Notation):
C12H15NO7
CAS Number:
Molecular Weight:
285.25
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
Assay
≥99% (TLC)
storage temp.
−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
InChI key
SWRPIVXPHLYETN-UHFFFAOYSA-N
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Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (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
Using networks to identify fine structural differences between functionally distinct protein states.
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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