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Human 5-hydroxytryptamine (serotonin) receptor 1F (HTR1F) ACTOne Stable Cell Line
Human 5-hydroxytryptamine (serotonin) receptor 1F (HTR1F) ACTOne Stable Cell Line
- 中文名称：
- Human 5-hydroxytryptamine (serotonin) receptor 1F (HTR1F) ACTOne Stable Cell Line
- 英文名称：
- Human 5-hydroxytryptamine (serotonin) receptor 1F (HTR1F) ACTOne Stable Cell Line
- 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：
- AAA62072
- 规格：
- INQUIRE
- 保存建议：
- Dry Ice Shipment: Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
Shipping Note: Product is available for shipment in the United States, Canada and European countries. Please inquire for shipment to other countries.
- 货期：
- 6-8周
- CAS号：
- 620-72-4
- 纯度：
- N/A
- 产品形式：
- N/A
- 分子量：
- 215.05 g/mol
- 分子式：
- C8H7BrO2
- 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：
Background/Introduction: Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions-including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now known to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase(3). When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immune-oadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (7).
