[Latin Name] Sophora Japonica L

[Plant Source] from China

[Specifications] 90%-99%

[Appearance] Yellow crystalline powder

Plant Part Used:Bud

[Particle size] 80 Mesh

[Loss on drying] ≤12.0%

[Heavy Metal] ≤10PPM

[Storage] Store in cool & dry area, keep away from the direct light and heat.

[Shelf life] 24 Months

[Package] Packed in paper-drums and two plastic-bags inside.

[Net weight] 25kgs/drum

Brief Introduction

Quercetin is a plant pigment (flavonoid). It is found in many plants and foods, such as red wine, onions, green tea, apples, berries, Ginkgo biloba, St. John’s wort, American elder, and others. Buckwheat tea has a large amount of quercetin. People use quercetin as a medicine.

Quercetin is used for treating conditions of the heart and blood vessels including “hardening of the arteries” (atherosclerosis), high cholesterol, heart disease, and circulation problems. It is also used for diabetes, cataracts, hay fever, peptic ulcer, schizophrenia, inflammation, asthma, gout, viral infections, chronic fatigue syndrome (CFS), preventing cancer, and for treating chronic infections of the prostate. Quercetin is also used to increase endurance and improve athletic performance.

Main Function

1.Quercetin may expel phlegm and arrest coughing, it can also be used as anti-asthmatic.

2. Quercetin has anticancer activity, inhibits PI3-kinase activity and slightly inhibits PIP Kinase activity, reduces cancer cell growth via type II estrogen receptors.

3.Quercetin may inhibit histamine release from basophils and mast cells.

4. Quercetin may control the spread of certain viruses within the body.

5, Quercetin may help reduce tissue destruction.

6.Quercetin may also be beneficial in the treatment of dysentery, gout, and psoriasis

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CX3CR1 Is Expressed in Differentiated Human Ciliated Airway Cells and Co-Localizes with Respiratory Syncytial Virus on Cilia in a G Protein-Dependent Manner. Kwang-Il Jeong et al (2015), PLoS ONE https://dx.doi.org/10.1371/journal.pone.0130517

Respiratory syncytial virus (RSV) is the principal cause of bronchiolitis in infants and a significant healthcare problem. The RSV Glycoprotein (G) mediates attachment of the virus to the cell membrane, which facilitates interaction of the RSV Fusion (F) protein with nucleolin, thereby triggering fusion of the viral and cellular membranes. However, a host protein ligand for G has not yet been identified. Here we show that CX3CR1 is expressed in the motile cilia of differentiated human airway epithelial (HAE) cells, and that CX3CR1 co-localizes with RSV particles. Upon infection, the distribution of CX3CR1 in these cells is significantly altered. Complete or partial deletion of RSV G results in viruses binding at least 72-fold less efficiently to cells, and reduces virus replication. Moreover, an antibody targeting an epitope near the G protein’s CX3CR1-binding motif significantly inhibits binding of the virus to airway cells. Given previously published evidence of the interaction of G with CX3CR1 in human lymphocytes, these findings suggest a role for G in the interaction of RSV with ciliated lung cells. This interpretation is consistent with past studies showing a protective benefit in immunizing against G in animal models of RSV infection, and would support targeting the CX3CR1-G protein interaction for prophylaxis or therapy. CX3CR1 expression in lung epithelial cells may also have implications for other respiratory diseases such as asthma.