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149649-90-1

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149649-90-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 149649-90-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,9,6,4 and 9 respectively; the second part has 2 digits, 9 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 149649-90:
(8*1)+(7*4)+(6*9)+(5*6)+(4*4)+(3*9)+(2*9)+(1*0)=181
181 % 10 = 1
So 149649-90-1 is a valid CAS Registry Number.

149649-90-1SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name O-(3-phenyl-2-propynyl)hydroxylamine

1.2 Other means of identification

Product number -
Other names O-(3-Phenyl-prop-2-ynyl)-hydroxylamine

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:149649-90-1 SDS

149649-90-1Relevant articles and documents

Iodocyclization of hydroxylamine derivatives based on the control of oxidative aromatization leading to 2,5-dihydroisoxazoles and isoxazoles

Okitsu, Takashi,Sato, Kana,Potewar, Taterao M.,Wada, Akimori

experimental part, p. 3438 - 3449 (2011/06/26)

An efficient method for the synthesis of 2,5-dihydroisoxazoles and isoxazoles using iodocyclization of N-alkoxycarbonyl O-propargylic hydroxylamines has been developed. 2,5-Dihydro-4-iodoisoxazole underwent the cross-coupling reactions without aromatization to afford polyfunctionalized 2,5-dihydroisoxazoles. This process was applied to the preparation of valdecoxib and its 2,5-dihydro-derivative.

Synthesis and biological characterization of 1,4,5,6- tetrahydropyrimidine and 2-amino-3,4,5,6-tetrahydropyridine derivatives as selective m1 agonists

Messer Jr., William S.,Abuh, Yahaya F.,Liu, Yang,Periyasamy, Sumudra,Ngur, Dan O.,Edgar, Michael A. N.,El-Assadi, Afif A.,Sbeih, Sbeih,Dunbar, Philip G.,Roknich, Scott,Rho, Taikyun,Fang, Zheng,Ojo, Babatunde,Zhang, Hao,Huzl III, James J.,Nagy, Peter I.

, p. 1230 - 1246 (2007/10/03)

Previous studies identified several novel tetrahydropyrimidine derivatives exhibiting muscarinic agonist activity in rat brain. Such compounds might be useful in treating cognitive and memory deficits associated with low acetylcholine levels, as found in Alzheimer's disease. To determine the molecular features of ligands important for binding and activity at muscarinic receptor subtypes, the series of tetrahydropyrimidines was extended. Several active compounds were examined further for functional selectivity through biochemical studies of muscarinic receptor activity using receptor subtypes expressed in cell lines. Several amidine derivatives displayed high efficacy at m1 receptors and lower activity at m3 receptors coupled to phosphoinositide (PI) metabolism in A9 L cells. Four ligands, including 1b, 1f, 2b, and 7b, exhibited marked functional selectivity for m1 vs m3 receptors. Compound 1f also exhibited low activity at m2 receptors coupled to the inhibition of adenylyl cyclase in A9 L cells. Molecular modeling studies also were initiated to help understand the nature of the interaction of muscarinic agonists with the m1 receptor using a nine amino model of the m1 receptor. Several important interactions were identified, including interactions between the ester moiety and Thr192. Additional interactions were found for oxadiazoles and alkynyl derivatives with Asn382, suggesting that enhanced potency and selectivity may be achieved by maximizing interactions with Asp105, Thr192, and Ash382. Taken together, the data indicate that several amidine derivatives display functional selectivity for m1 muscarinic receptors, warranting further evaluation as therapeutic agents for the treatment of Alzheimer's disease. In addition, several amino acid residues were identified as potential binding sites for m1 agonists. These data may be useful in directing efforts to develop even more selective m1 agonists.

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