Detecting HSP90 phosphorylation.
Detecting HSP90 phosphorylation.
复制标题
检测 HSP90 磷酸化。
DOI：
10.1007/978-1-61779-295-3_5
复制
发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Neckers,Len
中科院分区：
文献类型：
--
作者：
Mollapour,Mehdi;Neckers,Len
热休克蛋白90（HSP 90）是真核生物中一种重要的分子伴侣。HSP 90的ATP酶活性与其分子伴侣的功能密切相关。辅分子伴侣以及翻译后修饰（磷酸化、乙酰化和S-亚硝基化）对于调节其ATP酶活性是重要的。酵母可用于表达和纯化HSP 90，并可通过泛磷酸丝氨酸或磷酸苏氨酸抗体检测其磷酸化。
Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis.HSP90’s ATPase activity is associated with its chaperone function. Co-chaperones as well as posttranslational modifications (phosphorylation, acetylation, andS-nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purifyHSP90and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.