Hydrocinnamic acid

Hydrocinnamic acid
Product Name Hydrocinnamic acid
CAS No.: 501-52-0
Catalog No.: CFN96158
Molecular Formula: C9H10O2
Molecular Weight: 150.2 g/mol
Purity: >=98%
Type of Compound: Phenylpropanoids
Physical Desc.: Powder
Source: The herbs of Piper nigrum
Solvent: Chloroform, Dichloromethane, Ethyl Acetate, DMSO, Acetone, etc.
Price: $70/1g
Hydrocinnamic acid inhibits the currents of WT and SQT3 syndrome-related mutants of Kir2.1 channel.
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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

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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    J Sci Food Agric. 2013 Jan 15;93(1):134-41.
    Salt effect on phenolics and antioxidant activities of Tunisian and Canadian sweet marjoram (Origanum majorana L.) shoots.[Pubmed: 22674342]
    Two varieties of Origanum majorana (Canadian and Tunisian) were evaluated for their phenolic, flavonoid and tannin contents, individual phenolic compounds and antioxidant activities under NaCl constraint.
    METHODS AND RESULTS:
    The results showed a significant variability in phenolic composition and antioxidant behavior between the two varieties under salt stress. The phenolic composition of methanolic extracts was determined by reversed-phase high-performance liquid chromatography. Amentoflavone was the predominant flavonoid compound; in addition, trans-2-Hydrocinnamic acid became the major phenolic acid with salt treatment of the Tunisian variety. In the control, Canadian variety extract was characterized by high levels of gallic acid and amentoflavone. However, under 75 mmol L(-1) NaCl, gallic acid content doubled, whereas amentoflavone content was maintained in the Canadian variety. Stimulation of phenolic acid biosynthesis was observed in these two varieties under salt treatment despite the fact that shoots of the Tunisian variety showed higher antioxidant activities compared to those from the Canadian variety. Tunisian O. majorana might have developed tolerance to salinity and avoided tissue damage by activating enzymes involved in the galactosylation of quercetin into quercetin-3-galactoside and quercetin-3-rhamnoside.
    CONCLUSIONS:
    Our results confirmed the tolerance of Tunisian O. majorana plants.
    J Membr Biol. 2017 Oct;250(5):425-432.
    Hydrocinnamic Acid Inhibits the Currents of WT and SQT3 Syndrome-Related Mutants of Kir2.1 Channel.[Pubmed: 28660286]
    Gain of function in mutations, D172N and E299V, of Kir2.1 will induce type III short QT syndrome.
    METHODS AND RESULTS:
    In our previous work, we had identified that a mixture of traditional Chinese medicine, styrax, is a blocker of Kir2.1. Here, we determined a monomer, Hydrocinnamic acid (HA), as the effective component from 18 compounds of styrax. Our data show that HA can inhibit the currents of Kir2.1 channel in both excised inside-out and whole-cell patch with the IC50 of 5.21 ± 1.02 and 10.08 ± 0.46 mM, respectively. The time course of HA blockage and washout are 2.3 ± 0.6 and 10.5 ± 2.6 s in the excised inside-out patch. Moreover, HA can also abolish the currents of D172N and E299V with the IC50 of 6.66 ± 0.57 and 5.81 ± 1.10 mM for D172N and E299V, respectively. Molecular docking results determine that HA binds with Kir2.1 at K182, K185, and K188, which are phosphatidylinositol 4,5-bisphosphate (PIP2) binding residues.
    CONCLUSIONS:
    Our results indicate that HA competes with PIP2 to bind with Kir2.1 and inhibits the currents.
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