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Puerarin 6''-O-Xyloside Sale

(Synonyms: 葛根素-6″-O-木糖苷) 目录号 : GC37038

Puerarin 6''-O-Xyloside,是从葛根中分离得到的,拥有抗炎和抗癌活性。Puerarin 6''-O-Xyloside 可诱导线粒体介导的细胞凋亡通路。

Puerarin 6''-O-Xyloside Chemical Structure

Cas No.:114240-18-5

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1mg
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产品描述

Puerarin 6''-O-Xyloside, isolated from radix of Pueraria lobata (Willd.), possesses snti-osteoporotic and anti-tumor activity. Puerarin 6''-O-Xyloside induces the mitochondria-mediated apoptosis pathway.[1][2].

[1]. Li H, et al. Anti-osteoporotic activity of puerarin 6"-O-xyloside on ovariectomized mice and its potential mechanism. Pharm Biol. 2016;54(1):111-7. [2]. Chen T, et al. In vitro and in vivo antitumour activities of puerarin 6″-O-xyloside on human lung carcinoma A549 cell line via the induction of the mitochondria-mediated apoptosis pathway. Pharm Biol. 2016 Sep;54(9):1793-9.

Chemical Properties

Cas No. 114240-18-5 SDF
别名 葛根素-6″-O-木糖苷
Canonical SMILES OC1=CC=C2C(OC=C(C3=CC=C(O)C=C3)C2=O)=C1[C@@H]([C@@H]([C@@H](O)[C@@H]4O)O)O[C@@H]4CO[C@H](OC[C@@H](O)[C@@H]5O)[C@@H]5O
分子式 C26H28O13 分子量 548.49
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 1.8232 mL 9.1159 mL 18.2319 mL
5 mM 0.3646 mL 1.8232 mL 3.6464 mL
10 mM 0.1823 mL 0.9116 mL 1.8232 mL
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Research Update

Ionic-liquid-based ultrasound-assisted extraction combined with countercurrent chromatography and semipreparative LC for the preparation of monoamine oxidase B inhibitors from Pueraria thomsonii

J Sep Sci 2022 Mar;45(5):1116-1127.PMID:34967131DOI:10.1002/jssc.202100799.

A simple and efficient method was developed for the rapid screening and identification of ligands for monoamine oxidase B. A new ionic-liquid-based ultrasound-assisted extraction method for medicinal herbs was also developed and validated. In addition, the hyphenated technique of countercurrent chromatography and semipreparative-LC was developed and applied to the isolation of the chemical constituents for Pueraria thomsonii Benth. Three potent monoamine oxidase B inhibitors, namely, daidzein-4',7-diglucoside (42.2 mg), Puerarin 6''-O-Xyloside (88.3 mg), and 3'-hydroxypuerarin (48.5 mg) with purities of 98.2, 96.3, and 97.1%, respectively, were obtained from 500 g of P. thomsonii raw material using semi-preparative high-performance liquid chromatography, whereas 3'-methoxypuerarin (76.2 mg), daidzein-8-C-apiosyl (1→6) glucoside (84.2 mg), and tectorigenin (75.1 mg) with purities of 98.5, 96.4, and 96.8%, respectively, were obtained from 500 g raw material via countercurrent chromatography using a two-phase solvent system comprising n-hexane-ethyl acetate-methanol-water at a volume ratio of 1.85:1.00:0.86:3.69 (v/v/v/v). Then, the anti-Alzheimer activity of the phytochemicals was assessed using a PC12 cell model. Treatment with tectorigenin, daidzein-4',7-diglucoside, Puerarin 6''-O-Xyloside, 3'-hydroxypuerarin, 3'-methoxypuerarin, and daidzein-8-C-apiosyl (1→6) glucoside (100 μg/mL), resulted in cell viabilities of 69.00, 65.81, 59.69, 57.90, 55.61, and 54.59%, respectively (p < 0.001). The protocol was proved to be very accurate and efficient.

Screening of inhibitors against histone demethylation jumonji domain-containing protein 3 by capillary electrophoresis

J Chromatogr A 2020 Feb 22;1613:460625.PMID:31668999DOI:10.1016/j.chroma.2019.460625.

Jumonji domain-containing proteins (JMJDs) play an important role in the epigenetic regulation of gene expression. Aberrant regulation of histone modification has been observed in the progression of a variety of diseases, such as neurological disorders and cancer. Therefore, discovery of selective modulators of JMJDs is very attractive in new drug discovery. Herein, a simple capillary electrophoresis (CE) method was developed for screening of inhibitors against JMJD3. A known JMJD3 inhibitor GSK-J1, 5-carboxyfluorescein labeled substrate peptide with an amino acid sequence of KAPRKQLATKAARK(me3)SAPATGG (truncated from histone H3), as well as a small chemical library composed of 37 purified natural compounds and 30 natural extracts were used for method development and validation. The separation of substrate from its demethylated product was achieved by addition of polycation hexadimethrine bromide (HDB) in the running buffer. The enzyme activity was thus assayed accurately through separating the demethylated product from the substrate and then measuring the peak area of the product. The enzyme inhibition can be read out by comparing the peak area of the demethylated product obtained in the present of inhibitors and that of the negative control in the absence of any inhibitor. The merit of the method is proved by discovering two new JMJD3 inhibitors: salvianic acid A and Puerarin 6''-O-Xyloside.