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Human Respiratory Syncytial Virus (Rsv) Fusion Glycoprotein, Rsv-F Primacu ELISA Kit
Human Respiratory Syncytial Virus (Rsv) Fusion Glycoprotein, Rsv-F Primacu ELISA Kit
- 中文名称：
- Human Respiratory Syncytial Virus (Rsv) Fusion Glycoprotein, Rsv-F Primacu ELISA Kit
- 英文名称：
- Human Respiratory Syncytial Virus (Rsv) Fusion Glycoprotein, Rsv-F Primacu ELISA Kit
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA124120
- 规格：
- 96-Strip-Wells|2x96-Strip-Wells|5x96-Strip-Wells
- 保存建议：
- Store at 2-8 degree C
- 货期：
- 6-8周
- 检测种属：
- Human
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. The G protein mediates attachment of the virus to cell surface receptors, while the F protein promotes fusion of the viral and cellular membranes, allowing entry of the virus ribonucleoprotein into the cell cytoplasm. The fusion (F) protein of RSV is synthesized as a nonfusogenic precursor protein (F), which during its migration to the cell surface is activated by cleavage into the disulfide-linked F1 and F2 subunits. This fusion is pH independent and occurs directly at the outer cell membrane, and the F2 subunit was identifed as the major determinant of RSV host cell specificity. The trimer of F1-F2 interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and induces the fusion between host cell and virion membranes. Notably, RSV fusion protein is unique in that it is able to interact directly with heparan sulfate and therefore is sufficient for virus infection. Furthermore, the fusion protein is also able to trigger p53-dependent apoptosis.
