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20691-92-3

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20691-92-3 Usage

Chemical Properties

Colourless liquid

Check Digit Verification of cas no

The CAS Registry Mumber 20691-92-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,0,6,9 and 1 respectively; the second part has 2 digits, 9 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 20691-92:
(7*2)+(6*0)+(5*6)+(4*9)+(3*1)+(2*9)+(1*2)=103
103 % 10 = 3
So 20691-92-3 is a valid CAS Registry Number.
InChI:InChI=1/C7H12N2/c1-9-4-2-7(6-8)3-5-9/h7H,2-5H2,1H3

20691-92-3SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name 1-methylpiperidine-4-carbonitrile

1.2 Other means of identification

Product number -
Other names 1-Methyl-piperidine-4-carbonitrile

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:20691-92-3 SDS

20691-92-3Relevant articles and documents

Protein Modification at Tyrosine with Iminoxyl Radicals

Ishiyama, Takashi,Kanai, Motomu,Maruyama, Katsuya,Oisaki, Kounosuke,Sakai, Kentaro,Seki, Yohei,Togo, Takaya

supporting information, p. 19844 - 19855 (2021/11/30)

Post-translational modifications (PTMs) of proteins are a biological mechanism for reversibly controlling protein function. Synthetic protein modifications (SPMs) at specific canonical amino acids can mimic PTMs. However, reversible SPMs at hydrophobic amino acid residues in proteins are especially limited. Here, we report a tyrosine (Tyr)-selective SPM utilizing persistent iminoxyl radicals, which are readily generated from sterically hindered oximes via single-electron oxidation. The reactivity of iminoxyl radicals with Tyr was dependent on the steric and electronic demands of oximes; isopropyl methyl piperidinium oxime 1f formed stable adducts, whereas the reaction of tert-butyl methyl piperidinium oxime 1o was reversible. The difference in reversibility between 1f and 1o, differentiated only by one methyl group, is due to the stability of iminoxyl radicals, which is partly dictated by the bond dissociation energy of oxime O-H groups. The Tyr-selective modifications with 1f and 1o proceeded under physiologically relevant, mild conditions. Specifically, the stable Tyr-modification with 1f introduced functional small molecules, including an azobenzene photoswitch, to proteins. Moreover, masking critical Tyr residues by SPM with 1o, and subsequent deconjugation triggered by the treatment with a thiol, enabled on-demand control of protein functions. We applied this reversible Tyr modification with 1o to alter an enzymatic activity and the binding affinity of a monoclonal antibody with an antigen upon modification/deconjugation. The on-demand ON/OFF switch of protein functions through Tyr-selective and reversible covalent-bond formation will provide unique opportunities in biological research and therapeutics.

5-HT3 receptor agonist, novel thiazole derivative and intermediate thereof

-

, (2008/06/13)

A 5-HT3 receptor against containing a thiazole derivative as the effective ingredient is provided and is represented by the Formula (I): STR1 wherein the A ring is substituted or unsubstituted and represents a benzene or a heterocyclic ring with one or two heteroatoms; one of L1 or L2 represents a single bond and the other is non-existent or represents an alkylene or alkenylene group; R represents: STR2

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