Heat Shock Protein
Heat shock proteins are present in cells under normal conditions, but are expressed at much higher levels under conditions of stress, such as pH change, oxygen deprivation, and heat. They function as molecular chaperones by stabilizing denatured proteins that have become misfolded or unfolded as a result of cellular stress and by aiding in their re-folding. Left uncorrected, these misfolded proteins can form aggregates that eventually can kill the cell.
Two isoforms of heat shock proteins, HSP90α and HSP90β, are integral to the folding and stabilization of over 50 proteins directly related to tumor growth, making HSP90 a promising target for the development of anti-cancer therapeutics. HSP90 inhibitors that bind the N-terminal, ATP binding pocket of HSP90 have resulted in a number of first and second generation anti-cancer drugs. Evidence suggests that targeting the C-terminal domain will lead to the identification of new and innovative drug candidates.
BPS’ portfolio of HSPs includes the first domain-specific HSP90 assay kits, enabling researchers to differentiate between inhibitors of the N- and C terminal domains of HSP90α and HSP90β. In addition to assay kits, BPS also offers purified HSP proteins, inhibitors, and screening and profiling services for HSP90 inhibitors.
1. Kamal, A. et al., Nature, 2003; 425: 407-410.
2. Neckers, L., et al., Trends Mol. Med. 2002; 8: S55-S61.