- 中文名称
热休克蛋白90 抗体
- 英文名字
- HSP90 (P. falciparum) Antibody: Dylight 405
- 供应商
- StressMarq
- 产品货号
- SPC-187D-DY405
- 产品报价
- ￥已停产
- 产品说明书
- 点击查看
- 购买方式
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- 产品新闻
- 背景资料
- HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms A and B, which share 85% sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90A exists predominantly as a homodimer while HSP90B exists mainly as a monomer.(2) From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). The number of proteins now know 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.5 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 adsorption 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 (9). Recently, Prof. Tatu’s laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. Falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at HSP90.ca.
- 应用类型
- WB | ICC/IF | IP
- 免疫原
- 重组全长PfHsp90
- 来源宿主
- 兔
- 反应性
- 恶性疟原虫
- 保存建议
- 厂家推荐蓝冰运输。收到产品后建议保存于-20ºC。
- 其他
- StressMarq Biosciences Inc. 在2007年成立于加拿大维多利亚，是一家生物科技公司，专门从事试剂与试剂盒研究，服务范围遍及3442多个国家。 StressMarq公司的核心技术领域为细胞应激（尤其是热休克蛋白（HSP）领域，领先全球），离子通道，载体研究，同时在神经科学领域推出特有的具有生物活性的Tau蛋白与A-突触核蛋白。产品领域涉及到：细胞凋亡、细胞信号、通路和转运、细胞器标志物、热休克、神经生物学、神经科学、氧化应激、磷酸化运输等。除了提供用于进一步研究的相关工具外，Str
- 注意
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该页面的中文产品信息的翻译，仅供参考。准确的产品信息请以厂家的英文说明书为准。下单前，请浏览说明书确认。
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