[Latin Name]  Citrus aurantium L.

[Specification] Synephrine 4.0%–80%

[Appearance] Yellow brown powder

Plant Part Used: Fruit

[Particle size] 80Mesh

[Loss on drying] ≤5.0%

[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

[What is Citrus Aurantium]

Citrus aurantium L, belonging to the family Rutaceae, is widely distributed in China. Zhishi, the Chinese traditional name for Citrus aurantium, has long been a folk medicine in traditional Chinese medicine (TCMto improve indigestion and help stimulate the Qi (energy force).

[Function]

1. Have the function of antioxidant, anti-inflammatory, hypolipidemic, vasoprotective and anticarcinogenic and cholesterol lowering actions.

2. Have the function of inhibiting following enzymes: Phospholipase A2, lipoxygenase, HMG-CoA reductase and cyclo-oxygenase.

3. Have the function of improving the health of capillaries by reducing the capillary permeability.

4. Have the function of reducing hay fever and other allergic conditions by inhibiting the release of histamine from mast cells. The possible activity of hesperidin could be explained by the inhibition of polyamine synthesis. (bitter orange extract)

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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