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Coniferin is a monosaccharide derivative that consists of coniferol attached to a beta-D-glucopyranosyl residue at position 1 through a glycosidic linkage.

531-29-3

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531-29-3 Usage

Uses

Used in Pharmaceutical Industry:
Coniferin is used as a pharmaceutical compound for its potential therapeutic properties. It can be utilized in the development of drugs targeting various health conditions due to its unique chemical structure and functional groups.
Used in Chemical Industry:
Coniferin can be employed as a chemical intermediate in the synthesis of other bioactive compounds and materials. Its ability to form glycosidic linkages allows it to be a valuable component in creating complex organic molecules for various applications.
Used in Food Industry:
Coniferin may be used as a natural sweetener or flavor enhancer in the food industry. Its monosaccharide derivative nature could provide a unique taste profile and potential health benefits when incorporated into food products.
Used in Cosmetic Industry:
In the cosmetic industry, coniferin could be utilized for its potential moisturizing and skin conditioning properties. Its ability to interact with biopolymers and macromolecules may contribute to improved skin hydration and overall skin health.

Check Digit Verification of cas no

The CAS Registry Mumber 531-29-3 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 5,3 and 1 respectively; the second part has 2 digits, 2 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 531-29:
(5*5)+(4*3)+(3*1)+(2*2)+(1*9)=53
53 % 10 = 3
So 531-29-3 is a valid CAS Registry Number.
InChI:InChI=1/C16H22O8/c1-22-11-7-9(3-2-6-17)4-5-10(11)23-16-15(21)14(20)13(19)12(8-18)24-16/h2-5,7,12-21H,6,8H2,1H3/b3-2+/t12-,13-,14+,15-,16-/m1/s1

531-29-3SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name coniferin

1.2 Other means of identification

Product number -
Other names Coniferin

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:531-29-3 SDS

531-29-3Downstream Products

531-29-3Relevant academic research and scientific papers

Anti-inflammatory terpenes from Schefflera rubriflora C. J. Tseng & G. Hoo with their TNF-α and IL-6 inhibitory activities

Li, Fenghua,Zhang, Jian,Lin, Mingbao,Su, Xianming,Li, Changkang,Wang, Hongqing,Li, Baoming,Chen, Ruoyun,Kang, Jie

, p. 23 - 32 (2019/04/26)

The 95% ethanol extract and its EtOAc and n-BuOH fractions obtained from the leaves and twigs of Schefflera rubriflora C. J. Tseng & G. Hoo showed significant inhibitory activities (33.6%, 35.7% and 40.6%, respectively) against croton oil-induced ear inflammation in mice. Bioactivity-guided isolation and separation gave eight previously undescribed terpenes or terpene glycosides. Structural elucidation was based on UV, IR, and NMR spectroscopy, MS, experimental and calculated ECD data, and Mosher's method. To identify anti-inflammatory components from the extract, all the compounds were evaluated for tumor necrosis factor-α (TNF-α) and interleukine-6 (IL-6) inhibitory activities. Four undescribed compounds inhibited mRNA expression of TNF-α and IL-6 with IC50 values of 15.3–52.4 μM.

Oxidation of monolignols by members of the berberine bridge enzyme family suggests a role in plant cell wall metabolism

Daniel, Bastian,Pavkov-Keller, Tea,Steiner, Barbara,Dordic, Andela,Gutmann, Alexander,Nidetzky, Bernd,Sensen, Christoph W.,Van Der Graaff, Eric,Wallner, Silvia,Gruber, Karl,Macheroux, Peter

, p. 18770 - 18781 (2015/08/04)

Plant genomes contain a large number of genes encoding for berberine bridge enzyme (BBE)-like enzymes. Despite the wide-spread occurrence and abundance of this protein family in the plant kingdom, the biochemical function remains largely unexplored. In this study, we have expressed two members of the BBE-like enzyme family from Arabidopsis thaliana in the host organism Komagataella pastoris. The two proteins, termed AtBBE-like 13 and AtBBE-like 15, were purified, and their catalytic properties were determined. In addition, AtBBE-like 15 was crystallized and structurally characterized by x-ray crystallography. Here, we show that the enzymes catalyze the oxidation of aromatic allylic alcohols, such as coumaryl, sinapyl, and coniferyl alcohol, to the corresponding aldehydes and that AtBBE-like 15 adopts the same fold as vanillyl alcohol oxidase as reported previously for berberine bridge enzyme and other FAD-dependent oxidoreductases. Further analysis of the substrate range identified coniferin, the glycosylated storage form of coniferyl alcohol, as a substrate of the enzymes, whereas other glycosylated monolignols were rather poor substrates. A detailed analysis of the motifs present in the active sites of the BBE-like enzymes in A. thaliana suggested that 14 out of 28 members of the family might catalyze similar reactions. Based on these findings, we propose a novel role of BBE-like enzymes in monolignol metabolism that was previously not recognized for this enzyme family.

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