[Latin Name] Corynante Yohimbe

[Plant Source] Yohimbe bark collected from Africa

[Specifications] Yohimbine 8% (HPLC)

[Appearance] Red Brown 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. Net weight:25kgs/drum

[What is yohimbe]

Yohimbe is a tree that grows in Africa, and the natives there have used the crude bark and purified compound to enhance sexual desire and performance. Yohimbe has been used for centuries as an aphrodisiac. It has even been smoked as a hallucinogen. Nowadays, Yohimbe bark extract is mostly used to treat impotence for men and women.

When ingested, Yohimbe is assimilated into the blood stream, and Yohimbe’s energizing effects come from its ability to increase blood flow to the genitals - and this applies to both men and women.Aside from its aphrodisiac effects, new research also show that Yohimbe has powerful antioxidant effects.

.

[Function]

Yohimbe Bark Extract Benefits£º

1.It’s an aphrodisiac for both men and women

2.Be used to fight impotence

3.It is shown to be a powerful antioxidant

4.It also helps prevent arteries from getting clogged

5.It helps sexual performance, increase libido

6.Ithas also been shown to help prevent heart attacks

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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