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        Detecting HSP90 Phosphorylation

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        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, and S -nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purify HSP90 and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.
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