1094070-51-5 Usage
General Description
Methyl 5-aminoisothiazole-3-carboxylate is a chemical compound with the molecular formula C6H7N3O2S. It is a derivative of aminoisothiazole and is commonly used as an intermediate in the synthesis of pharmaceuticals, agrochemicals, and other organic compounds. The compound has a heterocyclic ring structure and is a potential building block for the development of various drugs due to its pharmacological properties. Methyl 5-aminoisothiazole-3-carboxylate is also used as a reagent in organic chemical reactions and is an important compound in the field of medicinal chemistry.
Check Digit Verification of cas no
The CAS Registry Mumber 1094070-51-5 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,0,9,4,0,7 and 0 respectively; the second part has 2 digits, 5 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 1094070-51:
(9*1)+(8*0)+(7*9)+(6*4)+(5*0)+(4*7)+(3*0)+(2*5)+(1*1)=135
135 % 10 = 5
So 1094070-51-5 is a valid CAS Registry Number.
1094070-51-5Relevant articles and documents
New geldanamycin derivatives with anti Hsp properties by mutasynthesis
Hermane, Jekaterina,Eichner, Simone,Mancuso, Lena,Schr?der, Benjamin,Sasse, Florenz,Zeilinger, Carsten,Kirschning, Andreas
supporting information, p. 5269 - 5278 (2019/06/07)
Mutasynthetic supplementation of the AHBA blocked mutant strain of S. hygroscopicus, the geldanamycin producer, with 21 aromatic and heteroaromatic amino acids provided new nonquinoid geldanamycin derivatives. Large scale (5 L) fermentation provided four new derivatives in sufficient quantity for full structural characterisation. Among these, the first thiophene derivative of reblastatin showed strong antiproliferative activity towards several human cancer cell lines. Additionally, inhibitory effects on human heat shock protein Hsp90α and bacterial heat shock protein from H. pylori HpHtpG were observed, revealing strong displacement properties for labelled ATP and demonstrating that the ATP-binding site of Hsps is the target site for the new geldanamycin derivatives.
