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1202-41-1

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1202-41-1 Usage

Description

3,4-Dihydroxycinnamamide, also known as 3,4-DHCA, is a chemical compound with the molecular formula C9H9NO3. It is a derivative of cinnamic acid and features two hydroxyl groups and an amide group attached to the aromatic ring. These structural features confer upon it antioxidant and potential anti-inflammatory properties, making it a compound of interest in various fields of research and application.

Uses

Used in Pharmaceutical and Nutraceutical Industries:
3,4-Dihydroxycinnamamide is used as a potential therapeutic agent for various conditions due to its antioxidant and anti-inflammatory properties. It is being investigated for its potential applications in the treatment of cancer, Parkinson's disease, and diabetes, where its protective effects against oxidative stress and inflammation could be beneficial.
Used in Cosmetics Industry:
In the cosmetics industry, 3,4-Dihydroxycinnamamide is used as an active ingredient for skin protection and repair. Its antioxidant properties help to combat the harmful effects of free radicals, which can lead to skin aging and damage. Additionally, its potential anti-inflammatory effects may contribute to soothing and healing the skin.
Used in Research:
3,4-Dihydroxycinnamamide is also used in scientific research to explore its biological effects and potential uses further. Studies are being conducted to understand its mechanisms of action and to identify additional therapeutic applications where it may be beneficial.

Check Digit Verification of cas no

The CAS Registry Mumber 1202-41-1 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,2,0 and 2 respectively; the second part has 2 digits, 4 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 1202-41:
(6*1)+(5*2)+(4*0)+(3*2)+(2*4)+(1*1)=31
31 % 10 = 1
So 1202-41-1 is a valid CAS Registry Number.

1202-41-1SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name (E)-3-(3,4-dihydroxyphenyl)prop-2-enamide

1.2 Other means of identification

Product number -
Other names 3,4-dihydroxy-trans-cinnamic acid amide

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:1202-41-1 SDS

1202-41-1Downstream Products

1202-41-1Relevant articles and documents

Identification of cinnamic acid derivatives as novel antagonists of the prokaryotic proton-gated ion channel GLIC

Prevost, Marie S.,Delarue-Cochin, Sandrine,Marteaux, Justine,Colas, Claire,Van Renterghem, Catherine,Blondel, Arnaud,Malliavin, Thérèse,Corringer, Pierre-Jean,Joseph, Delphine

, p. 4619 - 4630 (2013/07/19)

Pentameric ligand gated ion channels (pLGICs) mediate signal transduction. The binding of an extracellular ligand is coupled to the transmembrane channel opening. So far, all known agonists bind at the interface between subunits in a topologically conserved "orthosteric site" whose amino acid composition defines the pharmacological specificity of pLGIC subtypes. A striking exception is the bacterial proton-activated GLIC protein, exhibiting an uncommon orthosteric binding site in terms of sequence and local architecture. Among a library of Gloeobacter violaceus metabolites, we identified a series of cinnamic acid derivatives, which antagonize the GLIC proton-elicited response. Structure-activity analysis shows a key contribution of the carboxylate moiety to GLIC inhibition. Molecular docking coupled to site-directed mutagenesis support that the binding pocket is located below the classical orthosteric site. These antagonists provide new tools to modulate conformation of GLIC, currently used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism.

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