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111709-57-0

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111709-57-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 111709-57-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,1,7,0 and 9 respectively; the second part has 2 digits, 5 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 111709-57:
(8*1)+(7*1)+(6*1)+(5*7)+(4*0)+(3*9)+(2*5)+(1*7)=100
100 % 10 = 0
So 111709-57-0 is a valid CAS Registry Number.

111709-57-0SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name 2,4,5,6(1H,3H)-Pyrimidinetetrone, 5-[(2-nitrophenyl)hydrazone] (en)

1.2 Other means of identification

Product number -
Other names 2,4,5,6-Tetraoxypyrimidine

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:111709-57-0 SDS

111709-57-0Downstream Products

111709-57-0Relevant articles and documents

Synthesis, activity evaluation, and docking analysis of barbituric acid aryl hydrazone derivatives as RSK2 inhibitors

Xue, Mengzhu,Xu, Minghao,Lu, Weiqiang,Huang, Jin,Li, Honglin,Xu, Yufang,Liu, Xiaofeng,Zhao, Zhenjiang

, p. 747 - 752 (2013/07/26)

The 90 kDa ribosomal S6 kinases (RSKs), especially RSK2, have attracted attention for the development of new anticancer agents. Through structural optimization of the hit compound 1 from our previous study, a series of barbituric acid aryl hydrazone analogues were designed and synthesized as potential RSK2 inhibitors. The most potent one, compound 9, showed a higher activity against RSK2 with an IC50 value of 1.95 μM. To analyze and elucidate their structure-activity relationship, the homology model of RSK2 N-terminal kinase domain was built and molecular docking simulations were performed, which provide helpful clues to design new inhibitors with desired activities.

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