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775351-90-1

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775351-90-1 Usage

General Description

Corylifol B is a chemical compound isolated from the seeds of the Psoralea corylifolia plant, also known as the babchi or bakuchiol plant. It belongs to the class of natural phenolic compounds and has been found to have various pharmacological properties, including anti-inflammatory, anti-cancer, anti-microbial, and hepatoprotective effects. Corylifol B has been the subject of scientific research for its potential therapeutic applications, particularly in traditional medicine systems such as Ayurveda and Traditional Chinese Medicine. It is known to exhibit antioxidant properties and has shown promising results in preclinical studies for its ability to inhibit the growth of cancer cells. The compound has also been investigated for its potential use in skincare and cosmetics due to its anti-aging and anti-inflammatory properties.

Check Digit Verification of cas no

The CAS Registry Mumber 775351-90-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 7,7,5,3,5 and 1 respectively; the second part has 2 digits, 9 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 775351-90:
(8*7)+(7*7)+(6*5)+(5*3)+(4*5)+(3*1)+(2*9)+(1*0)=191
191 % 10 = 1
So 775351-90-1 is a valid CAS Registry Number.

775351-90-1Downstream Products

775351-90-1Relevant articles and documents

Molecular Characterization and Phylogenetic Analysis of Two Novel Regio-specific Flavonoid Prenyltransferases from Morus alba and Cudrania tricuspidata

Wang, Ruishan,Chen, Ridao,Li, Jianhua,Liu, Xiao,Xie, Kebo,Chen, Dawei,Yin, Yunze,Tao, Xiaoyu,Xie, Dan,Zou, Jianhua,Yang, Lin,Dai, Jungui

, p. 35815 - 35825 (2014)

Prenylated flavonoids are attractive specialized metabolites with a wide range of biological activities and are distributed in several plant families. The prenylation catalyzed by prenyltransferases represents a Friedel-Crafts alkylation of the flavonoid skeleton in the biosynthesis of natural prenylated flavonoids and contributes to the structural diversity and biological activities of these compounds. To date, all identified plant flavonoid prenyltransferases (FPTs) have been identified in Leguminosae. In the present study two new FPTs, Morus alba isoliquiritigenin 3′-dimethylallyltransferase (MaIDT) and Cudrania tricuspidata isoliquiritigenin 3′-dimethylallyltransferase (CtIDT), were identified from moraceous plants M. alba and C. tricuspidata, respectively. MaIDT and CtIDT shared low levels of homology with the leguminous FPTs. MaIDT and CtIDT are predicted to be membrane-bound proteins with predicted transit peptides, seven transmembrane regions, and conserved functional domains that are similar to other homogentisate prenyltransferases. Recombinant MaIDT and CtIDT were able to regioselectively introduce dimethylallyl diphosphate into the A ring of three flavonoids with different skeleton types (chalcones, isoflavones, and flavones). Phylogenetic analysis revealed thatMaIDT and CtIDT are distantly related to their homologs in Leguminosae, which suggests that FPTs in Moraceae and Leguminosae might have evolved independently. MaIDT and CtIDT represent the first two non-Leguminosae FPTs to be identified in plants and could thus lead to the identification of additional evolutionarily varied FPTs in other non-Leguminosae plants and could elucidate the biosyntheses of prenylated flavonoids in various plants. Furthermore, MaIDT and CtIDT might be used for regiospecific prenylation of flavonoids to produce bioactive compounds for potential therapeutic applications due to their high efficiency and catalytic promiscuity.

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