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Binding of the geldanamycin derivative 17 DMAG to Hsp90 measured with fluorescence label and label free

For proper folding, many proteins involved in signal transduction pathways, cell cycle regulation and apoptosis depend upon the ATP dependent molecular chaperone Hsp90. Consequently Hsp90 turned out to be an attractive target for cancer therapeutics. In this study we demonstrate the binding of the geldanamycin derivative 17 DMAG to Hsp90 using Microscale Thermophoresis (MST). The study also highlights the high content information of the MST measurements as one important benefit of Microscale Thermophoresis.

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Interactions of Liposome embedded SNARE Proteins
Interactions of Liposome embedded SNARE Proteins

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Rapid and Precise Biosimilar Candidate Profiling by nanoDSF
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