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D8942

Dichlorophenyl-ABA

Name: Dichlorophenyl-ABA
Brand: SIGMA

≥98% (HPLC), solid

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):

C₁₃H₉Cl₂NO₂

CAS Number:

18201-65-5

Molecular Weight:

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

GHS07

Signal Word

Warning

Hazard Statements

H315,H319,H335

Precautionary Statements

P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338

Hazard Classifications

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

Target Organs

Respiratory system

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

Certificates of Analysis (COA)

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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture.

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

Protein aggregation and neurodegenerative disease.

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

Prevention of transthyretin amyloid disease by changing protein misfolding energetics.

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

An Assay for Screening Potential Drug Candidates for Alzheimer's Disease That Act as Chaperones of the Transthyretin and Amyloid-β Peptides Interaction.

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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