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Heat shock proteins: Search for novel inhibitors – as simple as that!

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Heat shock proteins (HSPs) are of significant importance for cells. Not only do they perform chaperone functions for correct protein folding, they also protect proteins from various types of stress. On the other hand, however, HSPs foster diseases such as cancer, Alzheimer's or malaria[1] due to the stabilizing effect on disease-associated proteins. Finding potent HSP inhibitors is therefore of fundamental importance.

Here we present a target-oriented multiplex protein microarray to identify novel inhibitors. Instead of wasting large amounts of proteins and potential inhibitors, just 300 pmol of protein is sufficient. The microarray assay is based on competitive displacement of fluorescently-labelled ATP on full-length human HSP90 and bacterial HtpG by the respective potential inhibitors.

Figure 1: The Microarray is based on immobilized HSPs attached to a nitrocellulose membrane. Potential inhibitors compete with dye-labelled ATP for HSPs active sites (ATP-binding pockets) (adapted and used by Courtesy of [1]).

Figure 1: The Microarray is based on immobilized HSPs attached to a nitrocellulose membrane. Potential inhibitors compete with dye-labelled ATP for HSPs active sites (ATP-binding pockets) (adapted and used by courtesy of [1]).

 

Questions or inquiries?

Dr. Buerk Schaefer

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Reference:

[1] Schax et al. (2014) Microarray-based screening of heat shock protein inhibitors. Journal of Biotechnology. 180:1.