HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins. HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis.

Heat shock protein 90kDa α family class B member 1 (HSP90AB1) is expressed in cancers and has a role in the infection of Japanese encephalitis virus. It also takes part in signal transduction pathways.

Supplied in 50 mM sodium phosphate, pH 7.0, 300 mM NaCl, 150 mM imidazole, 0.1 mM PMSF, 0.2 mM DTT, 25% glycerol.

After opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles.