[Latin Name] Cinnamomun camphcra

[Plant Source] It is extracted from Ginkgo Biloba Leaf.

[Specifications]

1, Ginkgo Biloba Extract 24/6

Total Ginkgo flavone glycosides 24%

Total terpene lactones 6%

2, Ginkgo Biloba Extract 24/6

Total Ginkgo flavone glycosides 24%

Total terpene lactones 6%

Ginkgolic acid 5ppm

3,CP2005

Total Ginkgo flavone glycosides 24%

Quercatin: kaemperol 0.8–1.5

Total terpene lactones 6%

Ginkgolic acid <5ppm

4.Germany Standard

Total Ginkgo Flavone Glycosides 22.0%-27%

Total Terpene Lactones 5.0%-7.0%

Bilobalides 2.6%-3.2%

Ginkgolic acid <1ppm

5.Water-Soluble Ginkgo Biloba Extract 24/6

Water Solubility: 5g Ginkgo Biloba Extract will be dissolved completely in 100g water

Total Ginkgo Flavone Glycosides 24.0%

Total Terpene Lactones 6.0%

Ginkgolic acid <5.0ppm

[Appearance] Light yellow fine powder

[Particle size] 80 Mesh

[Loss on drying] £ 5.0%

[Heavy Metal] £10PPM

[Extract solvents] Ethanol

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

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

[Function]

Expanding blood vessel, resisting insufficient blood and oxygen deficit, increasing blood flow, improving cerebral arteries and distal

blood flow. Promoting cerebral circulation metabolism, improving memory function, resisting depression, resisting lipidic overoxidation,

protecting liver damage.

In clinic, curing high blood pressure, hyperlipoidemia, coronary heart disease, angina pectoris, arterial sclerosis, cerebral embolism,

senile dementia, primary and periodic dropsy, acute drumming in the ears, epicophosis, a variety of body function in disorder, dizziness

and so on.

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.

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