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14131-64-7 Usage

Chemical Properties

white solid

Check Digit Verification of cas no

The CAS Registry Mumber 14131-64-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,1,3 and 1 respectively; the second part has 2 digits, 6 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 14131-64:
67 % 10 = 7
So 14131-64-7 is a valid CAS Registry Number.



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

Version: 1.0

Creation Date: Aug 14, 2017

Revision Date: Aug 14, 2017


1.1 GHS Product identifier

Product name N-[(2S,3R,4S,5R)-3,4,5,6-tetrahydroxy-1-oxohexan-2-yl]acetamide,hydrate

1.2 Other means of identification

Product number -
Other names -

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:14131-64-7 SDS

14131-64-7Relevant articles and documents

Synthesis and anti-acetylcholinesterase activities of novel glycosyl coumarylthiazole derivatives

Cao, Lian-Gong,Cao, Zhi-Ling,Jiang, Kai-Jun,Liu, Shu-Hao,Liu, Wei-Wei,Lu, Xing,Shao, Zhong-Bai,Shi, Da-Hua,Wang, Lei,Wang, You-Xian

, p. 359 - 364 (2020/12/28)

Eleven glycosyl coumarylthiazole derivatives are synthesized by cyclization and condensation of glycosyl thiourea with 3-bromoacetyl coumarins in ethanol. The reaction conditions are optimized and good yields of products (80%–95%) are obtained. The structures of all new products were confirmed by IR, 1H and 13C NMR, and by HRMS (electrospray ionization). The in vitro acetylcholinesterase (AChE) inhibitory activities of these new compounds are tested by Ellman’s method. Among them, N-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-4-(6-nitrocoumarinyl)-1,3-thiazole-2-amine showed the best activity with an in vitro AChE inhibitory rate of 58% and an IC50 value of 12 ± 0.38 μg/mL.

Synthesis and anticholinesterase activities of novel glycosyl benzoxazole derivatives

Cao, Zhi-Ling,Liu, Shu-Hao,Liu, Wei-Wei,Ren, Shu-Ting,Shi, Da-Hua,Wang, Lei,Wang, You-Xian,Wu, Yu-Ran

, p. 363 - 366 (2020/02/05)

Eight glycosyl benzoxazole derivatives are synthesized by nucleophilic addition reactions of glycosyl isothiocyanate with o-aminophenol in tetrahydrofuran. The reaction conditions are optimized, and good yields (86%–94%) were obtained. The structures of all new products are confirmed by infrared, 1H nuclear magnetic resonance, and high-resolution mass spectrometry (electrospray ionization). In addition, the in vitro cholinesterase inhibitory activities of these new compounds are tested by Ellman’s method.

Biochemical Characterization and Structural Analysis of a β- N-Acetylglucosaminidase from Paenibacillus barengoltzii for Efficient Production of N-Acetyl- d -glucosamine

Liu, Yihao,Jiang, Zhengqiang,Ma, Junwen,Ma, Shuai,Yan, Qiaojuan,Yang, Shaoqing

, p. 5648 - 5657 (2020/06/03)

Bioproduction of N-acetyl-d-glucosamine (GlcNAc) from chitin, the second most abundant natural renewable polymer on earth, is of great value in which chitinolytic enzymes play key roles. In this study, a novel glycoside hydrolase family-18 β-N-acetylglucosaminidase (PbNag39) from Paenibacillus barengoltzii suitable for GlcNAc production was identified and biochemically characterized. It possessed a unique shallow catalytic groove (5.8 ?) as well as a smaller C-terminal domain (solvent-accessible surface area, 5.1 × 103 ?2) and exhibited strict substrate specificity toward N-acetyl chitooligosaccharides (COS) with GlcNAc as the sole product, showing a typical manner of action of β-N-acetylglucosaminidases. Thus, an environmentally friendly bioprocess for GlcNAc production from ball-milled powdery chitin by an enzyme cocktail reaction was further developed. By using the new route, the powdery chitin conversion rate increased from 23.3% (v/v) to 75.3% with a final GlcNAc content of 22.6 mg mL-1. The efficient and environmentally friendly bioprocess may have great application potential in GlcNAc production.

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