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    Helicid
    Helicid
    Information
    CAS No. 80154-34-3 Price $30 / 20mg
    Catalog No.CFN99957Purity>=98%
    Molecular Weight284.26Type of CompoundPhenols
    FormulaC13H16O7Physical 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.
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    Biological Activity
    Description: 1. Helicid analogues are mushroom tyrosinase inhibitors, some of them have more potent inhibitory activities than arbutin (IC50 =7.3 mM).
    2. Some helicid analogues exhibit potent cholinesterase (AChE) inhibitory activities.
    Targets: AChR
    Helicid Description
    Source: The roots of Helicia erratica Hook. f.
    Solvent: DMSO, Pyridine, Methanol, Ethanol, 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.
    doi: 10.1016/j.phymed.2017.12.030.

    PMID: 29496173
    Calculate Dilution Ratios(Only for Reference)
    1 mg 5 mg 10 mg 20 mg 25 mg
    1 mM 3.5179 mL 17.5895 mL 35.1791 mL 70.3581 mL 87.9477 mL
    5 mM 0.7036 mL 3.5179 mL 7.0358 mL 14.0716 mL 17.5895 mL
    10 mM 0.3518 mL 1.759 mL 3.5179 mL 7.0358 mL 8.7948 mL
    50 mM 0.0704 mL 0.3518 mL 0.7036 mL 1.4072 mL 1.759 mL
    100 mM 0.0352 mL 0.1759 mL 0.3518 mL 0.7036 mL 0.8795 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.
    Helicid References Information
    Citation [1]

    Spectrochim Acta A Mol Biomol Spectrosc. 2014 Apr 24;124:46-51.

    Binding of helicid to human serum albumin: a hybrid spectroscopic approach and conformational study.[Pubmed: 24463239]
    The interaction between human serum albumin and Helicid was studied by steady-state fluorescence, ultraviolet-visible, circular dichroism, Fourier transform infrared techniques and molecular modeling. The binding site numbers, association constants, and corresponding thermodynamic parameters were used to investigate the quenching mechanism. The alternations of protein secondary structure in the presence of Helicid were demonstrated using synchronous fluorescence, Fourier transform infrared, circular dichroism and three-dimensional fluorescence spectra. The molecular modeling results revealed that Helicid could bind to hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. The binding site of Helicid in HSA was ascertained. Moreover, an apparent distance of 3.33 nm between the Trp214 and Helicid was obtained via fluorescence resonance energy transfer method.
    Citation [2]

    J Chromatogr B Analyt Technol Biomed Life Sci. 2015 Apr 15;988:8-12.

    Bioavailability and pharmacokinetics profile of helicid in beagle dogs using gradient elution high performance liquid chromatography electrospray ionization mass spectrometry.[Pubmed: 25743699]
    A simple, sensitive and reliable gradient elution high performance liquid chromatography electrospray ionization mass spectrometry (HPLC-ESI-MS) method was developed for quantifying Helicid in dog plasma. The limit of detection (LOD) and the lower limit of quantitation (LLOQ) were 0.3 and 1ng/mL, respectively. This method was validated for selectivity, linearity, accuracy and precision, extraction recoveries, matrix effects, carry-over, cross-talk, dilution integrity, stability and incurred sample reanalysis (ISR). Bioavailability and pharmacokinetic parameters of Helicid in beagle dogs were researched from a two period crossover design study. After intravenous administration (i.v.), Helicid had a mean (±SD) AUC0-∞ of 12062.06±2482.69ng/mLh and terminal half-life (t1/2z) of 2.91±1.37h, while Cmax was 35613.23±8157.18ng/mL. Following intragastric gavage administration (i.g.), AUC0-∞ was 7589.16±1797.20ng/mLh along with a longer t1/2z of 4.10±4.35h. Cmax was researched at 0.58±0.20h. The absolute bioavailability (F) of Helicid was 15.74±1.87%.
    Citation [3]

    Bioorg Med Chem Lett. 2008 Dec 15;18(24):6490-3.

    Synthesis and biological evaluation of helicid analogues as mushroom tyrosinase inhibitors.[Pubmed: 18996693 ]
    A series of Helicid analogues were synthesized and evaluated as tyrosinase inhibitors. The results demonstrated that some compounds had more potent inhibitory activities than arbutin (IC(50) 7.3 mM). In particular, compound 1c bearing 4,6-O-benzylidene substituent on the sugar moiety was found to be the most potent inhibitor with IC(50) value of 0.052 mM. The inhibition kinetics analyzed by Lineweaver-Burk plots revealed that Helicid analogues were competitive inhibitors. The Circular dichroism spectra indicated that those compounds induced conformational changes of mushroom tyrosinase upon binding.
    Citation [4]

    Eur J Med Chem. 2008 Jan;43(1):166-73.

    Synthesis and biological evaluation of helicid analogues as novel acetylcholinesterase inhibitors.[Pubmed: 17574306]
    A series of Helicid analogues were prepared and evaluated in vitro for the cholinesterase (AChE and BuChE) inhibitory activities via UV spectroscopy. The results indicated that compounds 5, 6d and 8 exhibited potent AChE inhibitory activities with IC(50) values of 0.45+/-0.02microM, 0.49+/-0.02microM, and 0.20+/-0.01microM, respectively. High selectivity for AChE over BuChE was also observed. Kinetic study showed that the mechanism of AChE inhibition of compounds 5, 6d and 8 was all mixed-type.