[Latin Name] Vaccinium myrtillus l.

[Plant Source] Wild bilberry fruit cultivated from Sweden & Finland

[Specifications]

1) Anthocyanidins 25% UV (Glycosyl removed)

2) Anthocyanins 25% HPLC

3) Anthocyanins 36% HPLC

[Particle size] 80 Mesh

[Loss on drying] ≤5.0%

[Heavy Metal] ≤10PPM

[Pesticide residue] EC396-2005, USP 34, EP 8.0, FDA

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

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

[General feature]

1. 100% extracted from European bilberry fruit, approved ID test from ChromaDex andAlkemist Lab;

2.Without any adultery of other relative species of Berries,such as Blueberry,  Mulberry,Cranberry,etc;

3. Pesticide residue: EC396-2005, USP 34, EP 8.0, FDA

4. Directly import the frozen fruit from North Europe;

5. Perfect water solubility,water insolubles<1.0%
6. Chromatographic fingerprint match EP6 requirement

[What is bilberry fruit]

Bilberry (Vaccinium Myrtillus L.) is a kind of perennial deciduous or evergreen fruit shrubs, mainly found in subarctic regions of the world as in Sweden, Finland and Ukraine, etc. Bilberries contain dense levels of anthocyanin pigments, which was said popularly to have been used by World War II RAF pilots to sharpen night vision. In fork medicine, Europeans have been taking bilberry for a hundred years. Bilberry extracts entered the healthcare market as a kind of dietary supplement for effects on vision enhancement and visual fatigue relief.

[Function]

Protect and regenerate rhodopsin and cure the eye diseases;

Prevent the cardiovascular diseases

Antioxidant and anti-aging

Softening blood capillary, enhancing the heart function and resisting cancer

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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