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1862237-99-7

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1862237-99-7 Usage

Molecular structure

2-((4,6-dimethylpyrimidin-2-yl)thio)-N-(5-(3-(prop-2-yn-1-yloxy)benzyl)thiazol-2-yl)acetamide is a complex compound containing a pyrimidine ring, a thiazole ring, and an acetamide group.

Substituents

The presence of methyl and prop-2-yn-1-yloxy groups adds to the molecular complexity of the compound.

Biological activity

The compound likely has biological activity due to the presence of thiazole and pyrimidine rings, which are commonly found in pharmaceutical drugs.

Pharmacological properties

The exact pharmacological properties of this chemical require further investigation to determine its potential therapeutic applications.

Toxicological properties

The toxicological properties of the compound are not yet known and require further research to understand its safety and potential side effects.

Potential applications

Due to its complex structure and the presence of biologically active rings, this compound may have potential applications in the pharmaceutical industry, but further research is needed to confirm its efficacy and safety.

Check Digit Verification of cas no

The CAS Registry Mumber 1862237-99-7 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,8,6,2,2,3 and 7 respectively; the second part has 2 digits, 9 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 1862237-99:
(9*1)+(8*8)+(7*6)+(6*2)+(5*2)+(4*3)+(3*7)+(2*9)+(1*9)=197
197 % 10 = 7
So 1862237-99-7 is a valid CAS Registry Number.

1862237-99-7Downstream Products

1862237-99-7Relevant articles and documents

Structure-based development of an affinity probe for sirtuin 2

Schiedel, Matthias,Rumpf, Tobias,Karaman, Berin,Lehotzky, Attila,Gerhardt, Stefan,Ovádi, Judit,Sippl, Wolfgang,Einsle, Oliver,Jung, Manfred

, p. 2252 - 2256 (2016)

Sirtuins are NAD+-dependent protein deacylases that cleave off acetyl groups, as well as other acyl groups, from the é?-amino group of lysines in histones and other substrate proteins. Dysregulation of human Sirt2 activity has been associated w

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