1. Csermely, P. et al: The 90-kDa molecular chaperone family: structure, function, and clinical applications. Pharmacol Ther. 1998 Aug;79(2):129-68.
2. Georgakis, G.V. et al: Heat-shock protein 90 inhibitors in cancer therapy: 17AAG and beyond. Future Oncol. 2005 Apr;1(2):273-81.
: 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 (1). 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 (2).
: Affinity chromatography
: Store at 4°C (add 0.1% NaN3
) for several months, and at -20°C for longer periods.
For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For optimal performance, avoid repeated handling and multiple freeze/thaw cycles.
: PBS pH 7.4, 0.02% sodium azide, 50% glycerol
: Synthetic peptide corresponding to amino acids 252-256 of human HSP90β
: Recognizes the HSP90β protein
: Western blot of human and mouse HSP90β
HSP90β from other species may also be detectable
||Sample Data : Representative western blot with Anti-HSP90β (1:1000) using 20ng of human recombinant HSP90α and HSP90β.
||Sample Data : Representative western blot with Anti-HSP90β (1:1000) using 3 μg, 10 μg, and 30 μg of HeLa cell lysate.
The Anti-HSP90 beta product can be utilized in the following research areas, but not limited to:
AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cellular Stress