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6303-46-4

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6303-46-4 Usage

General Description

6-chloro-N-(3,4-dichlorophenyl)pyrimidin-4-amine is a chemical compound with the molecular formula C10H6Cl3N3. It is a pyrimidine derivative with two chlorine atoms attached to the phenyl group. 6-chloro-N-(3,4-dichlorophenyl)pyrimidin-4-amine has potential applications in a variety of fields including pharmaceuticals, agrochemicals, and materials science. Its precise chemical properties and potential uses will depend on its specific applications and the context in which it is being utilized. Further research and testing will be necessary to fully understand the potential benefits and risks associated with this compound.

Check Digit Verification of cas no

The CAS Registry Mumber 6303-46-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 6,3,0 and 3 respectively; the second part has 2 digits, 4 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 6303-46:
(6*6)+(5*3)+(4*0)+(3*3)+(2*4)+(1*6)=74
74 % 10 = 4
So 6303-46-4 is a valid CAS Registry Number.

6303-46-4SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 13, 2017

Revision Date: Aug 13, 2017

1.Identification

1.1 GHS Product identifier

Product name (6-chloro-pyridin-3-yl)-piperidin-1-yl-methanone

1.2 Other means of identification

Product number -
Other names 2-chloro-5-(piperidin-1-ylcarbonyl)pyridine

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:6303-46-4 SDS

6303-46-4Relevant articles and documents

Development of a series of aryl pyrimidine kynurenine monooxygenase inhibitors as potential therapeutic agents for the treatment of Huntingtons disease

Toledo-Sherman, Leticia M.,Prime, Michael E.,Mrzljak, Ladislav,Beconi, Maria G.,Beresford, Alan,Brookfield, Frederick A.,Brown, Christopher J.,Cardaun, Isabell,Courtney, Stephen M.,Dijkman, Ulrike,Hamelin-Flegg, Estelle,Johnson, Peter D.,Kempf, Valerie,Lyons, Kathy,Matthews, Kimberly,Mitchell, William L.,Oconnell, Catherine,Pena, Paula,Powell, Kendall,Rassoulpour, Arash,Reed, Laura,Reindl, Wolfgang,Selvaratnam, Suganathan,Friley, Weslyn Ward,Weddell, Derek A.,Went, Naomi E.,Wheelan, Patricia,Winkler, Christin,Winkler, Dirk,Wityak, John,Yarnold, Christopher J.,Yates, Dawn,Munoz-Sanjuan, Ignacio,Dominguez, Celia

, p. 1159 - 1183 (2015/03/04)

We report on the development of a series of pyrimidine carboxylic acids that are potent and selective inhibitors of kynurenine monooxygenase and competitive for kynurenine. We describe the SAR for this novel series and report on their inhibition of KMO activity in biochemical and cellular assays and their selectivity against other kynurenine pathway enzymes. We describe the optimization process that led to the identification of a program lead compound with a suitable ADME/PK profile for therapeutic development. We demonstrate that systemic inhibition of KMO in vivo with this lead compound provides pharmacodynamic evidence for modulation of kynurenine pathway metabolites both in the periphery and in the central nervous system.

Binding or bending: Distinction of allosteric abl kinase agonists from antagonists by an NMR-based conformational assay

Jahnke, Wolfgang,Grotzfeld, Robert M.,Pelle, Xavier,Strauss, Andre,Fendrich, Gabriele,Cowan-Jacob, Sandra W.,Cotesta, Simona,Fabbro, Doriano,Furet, Pascal,Mestan, Juergen,Marzinzik, Andreas L.

supporting information; experimental part, p. 7043 - 7048 (2010/07/08)

Allosteric inhibitors of Bcr-Abl have emerged as a novel therapeutic option for the treatment of CML. Using fragment-based screening, a search for novel Abl inhibitors that bind to the myristate pocket was carried out. Here we show that not all myristate ligands are functional inhibitors, but that the conformational state of C-terminal helix-I is a structural determinant for functional activity. We present an NMR-based conformational assay to monitor the conformation of this crucial helix-I and show that myristate ligands that bend helix-I are functional antagonists, whereas ligands that bind to the myristate pocket but do not induce this conformational change are kinase agonists. Activation of c-Abl by allosteric agonists has been confirmed in a biochemical assay.

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