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    CAS No. 487-39-8 Price $198 / 20mg
    Catalog No.CFN90511Purity>=98%
    Molecular Weight372.41Type of CompoundLignans
    FormulaC21H24O6Physical DescriptionPowder
    Download Manual    COA    MSDSSimilar structuralComparison (Web)
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    Our products had been exported to the following research institutions and universities, And still growing.
  • Cornell University (USA)
  • Georgia Institute of Technology (USA)
  • Celltrion Chemical Research Inst... (Korea)
  • Kitasato University (Japan)
  • Warszawski Uniwersytet Medyczny (Poland)
  • University of Amsterdam (Netherlands)
  • University of Bordeaux (France)
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  • Macau University of Science and ... (China)
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    Featured Products
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    Biological Activity
    Description: Phillyrin, (+)-Phillygenin, and (-)-phillygenin exert the strongest inhibitory activities on NO production with IC(50) values.
    Targets: NO
    Phillygenin Description
    Source: The herbs of Forsythia suspensa.
    Solvent: Chloroform, Dichloromethane, Ethyl Acetate, DMSO, Acetone, etc.
    Storage: Providing storage is as stated on the product vial and the vial is kept tightly sealed, the product can be stored for up to 24 months(2-8C).

    Wherever possible, you should prepare and use solutions on the same day. However, if you need to make up stock solutions in advance, we recommend that you store the solution as aliquots in tightly sealed vials at -20C. Generally, these will be useable for up to two weeks. Before use, and prior to opening the vial we recommend that you allow your product to equilibrate to room temperature for at least 1 hour.

    Need more advice on solubility, usage and handling? Please email to: service@chemfaces.com

    After receiving: The packaging of the product may have turned upside down during transportation, resulting in the natural compounds adhering to the neck or cap of the vial. take the vial out of its packaging and gently shake to let the compounds fall to the bottom of the vial. for liquid products, centrifuge at 200-500 RPM to gather the liquid at the bottom of the vial. try to avoid loss or contamination during handling.
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    Recently, ChemFaces products have been cited in many studies from excellent and top scientific journals

    Cell. 2018 Jan 11;172(1-2):249-261.e12.
    doi: 10.1016/j.cell.2017.12.019.

    PMID: 29328914

    Mol Cell. 2017 Nov 16;68(4):673-685.e6.
    doi: 10.1016/j.molcel.2017.10.022.

    PMID: 29149595

    Scientific Reports 2017 Dec 11;7(1):17332.
    doi: 10.1038/s41598-017-17427-6.

    PMID: 29230013

    Molecules. 2017 Oct 27;22(11). pii: E1829.
    doi: 10.3390/molecules22111829.

    PMID: 29077044

    J Cell Biochem. 2018 Feb;119(2):2231-2239.
    doi: 10.1002/jcb.26385.

    PMID: 28857247

    Phytomedicine. 2018 Feb 1;40:37-47.

    PMID: 29496173
    Calculate Dilution Ratios(Only for Reference)
    1 mg 5 mg 10 mg 20 mg 25 mg
    1 mM 2.6852 mL 13.4261 mL 26.8521 mL 53.7043 mL 67.1303 mL
    5 mM 0.537 mL 2.6852 mL 5.3704 mL 10.7409 mL 13.4261 mL
    10 mM 0.2685 mL 1.3426 mL 2.6852 mL 5.3704 mL 6.713 mL
    50 mM 0.0537 mL 0.2685 mL 0.537 mL 1.0741 mL 1.3426 mL
    100 mM 0.0269 mL 0.1343 mL 0.2685 mL 0.537 mL 0.6713 mL
    * Note: If you are in the process of experiment, it's need to make the dilution ratios of the samples. The dilution data of the sheet for your reference. Normally, it's can get a better solubility within lower of Concentrations.
    Structure Identification:
    Spectrochim Acta A Mol Biomol Spectrosc. 2012 Jan;85(1):120-6.
    Interaction between phillygenin and human serum albumin based on spectroscopic and molecular docking.[Pubmed: 22000638]

    In this paper, the interaction of human serum albumin (HSA) with Phillygenin was investigated by fluorescence, circular dichroism (CD), UV-vis spectroscopic and molecular docking methods under physiological conditions. The Stern-Volmer analysis indicated that the fluorescence quenching of HSA by Phillygenin resulted from static mechanism, and the binding constants were 1.71×10(5), 1.61×10(5) and 1.47×10(4) at 300, 305 and 310K, respectively. The results of UV-vis spectra show that the secondary structure of the protein has been changed in the presence of Phillygenin. The CD spectra showed that HSA conformation was altered by Phillygenin with a major reduction of α-helix and an increase in β-sheet and random coil structures, indicating a partial protein unfolding. The distance between donor (HSA) and acceptor (Phillygenin) was calculated to be 3.52nm and the results of synchronous fluorescence spectra showed that binding of Phillygenin to HSA can induce conformational changes in HSA. Molecular docking experiments found that Phillygenin binds with HSA at IIIA domain of hydrophobic pocket with hydrogen bond interactions. The ionic bonds were formed with the O (4), O (5) and O (6) of Phillygenin with nitrogen of ASN109, ARG186 and LEU115, respectively. The hydrogen bonds are formed between O (2) of Phillygenin and SER419. In the presence of copper (II), iron (III) and alcohol, the apparent association constant K(A) and the number of binding sites of Phillygenin on HSA were both decreased in the range of 88.84-91.97% and 16.09-18.85%, respectively.
    In view of the evidence presented, it is expected to enrich our knowledge of the interaction dynamics of Phillygenin to the important plasma protein HSA, and it is also expected to provide important information of designs of new inspired drugs.