Barley Grass Powder

Key Words: Organic barley grass powder；Barley grass juice powder

[Latin Name] Hordeum vulgare L.

[Plant Source] Barley Grass

[Solubility] Free soluble in water

[Appearance] Green fine powder

Plant Part Used: Grass

[Particle size]100 Mesh-200Mesh

[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.

[Shelf life] 24 Months

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

[Net weight] 25kgs/drum

[What is Barley ?]

Barley is an annual grass. Barley grass is the leaf of the barley plant, as opposed to the grain. It is capable of growing in a wide range of climatic conditions. Barley grass has greater nutritional value if harvested at a young age.

[How does it work?]

The fiber in barley might lower cholesterol and blood pressure in people with high cholesterol. Barley may also reduce blood sugar and insulin levels. Barley seems to slow stomach emptying. This could help keep blood sugar stable and create a sensation of being full, which might help to control appetite.

[Function]

1. Improves energy naturally

2. Rich in antioxidants

3. Improves digestion & regularity

4. Alkalizes the internal body

5. Helps rebuild the immune system

6. Provides raw building blocks for hair, skin and nails

7. Contains detoxification and cleansing properties

8. Contains anti-inflammatory ingredients

9. Promotes clear thinking

10. Has anti-aging properties

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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