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D8942

Sigma-Aldrich

Dichlorophenyl-ABA

≥98% (HPLC), solid

Sinónimos:

2-[(3,5-Dichlorophenyl)amino]benzoic acid

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About This Item

Fórmula empírica (notación de Hill):
C13H9Cl2NO2
Número de CAS:
18201-65-5
Peso molecular:
282.12
MDL number:
MFCD07370135
UNSPSC Code:
12352200
PubChem Substance ID:
24724469

assay

≥98% (HPLC)

form

solid

color

white

solubility

DMSO: ~18 mg/mL at ~60 °C

storage temp.

2-8°C

SMILES string

OC(=O)c1ccccc1Nc2cc(Cl)cc(Cl)c2

InChI

1S/C13H9Cl2NO2/c14-8-5-9(15)7-10(6-8)16-12-4-2-1-3-11(12)13(17)18/h1-7,16H,(H,17,18)

InChI key

FNGSQOJHNAYHAT-UHFFFAOYSA-N

Gene Information

human ... TTR(7276)

Biochem/physiol Actions

Inhibitor of transthyretin amyloid fibril formation in vitro.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

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Natàlia Reixach et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(9), 2817-2822 (2004-02-26)
The transthyretin (TTR) amyloidoses are human diseases in which the misfolded TTR protein aggregates in tissues with subsequent visceral, peripheral, and autonomic nerve dysfunction. Recent reports have stressed the importance of oligomeric intermediates as major cytotoxic species in various forms
Christopher A Ross et al.
Nature medicine, 10 Suppl, S10-S17 (2004-07-24)
Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases are increasingly being realized to have common cellular and molecular mechanisms including protein aggregation and inclusion body formation. The aggregates
Per Hammarström et al.
Science (New York, N.Y.), 299(5607), 713-716 (2003-02-01)
Genetic evidence suggests that inhibition of amyloid fibril formation by small molecules should be effective against amyloid diseases. Known amyloid inhibitors appear to function by shifting the aggregation equilibrium away from the amyloid state. Here, we describe a series of
Ellen Y Cotrina et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 26(72), 17462-17469 (2020-08-08)
The protein transthyretin (TTR) modulates amyloid-β (Aβ) peptides deposition and processing and this physiological effect is further enhanced by treatment with iododiflunisal (IDIF), a small-molecule compound (SMC) with TTR tetramer stabilization properties, which behaves as chaperone of the complex. This

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