- Nov. 13, 2019
-- Thermal stress or elevated temperatures cause proteins to denature thereby resulting in the loss of function leading to disruption in protein homeostasis. All organisms express a class of proteins known as Heat Shock Proteins (HSPs) to circumvent this problem by stabilizing the protein structure during stressful conditions. The name "Heat Shock Protein" comes from the original discovery that the abundance of these proteins is elevated during heat stress. Although HSPs are constitutively expressed and are involved in protein stabilization by ensuring the correct folding of newly synthesized proteins, their abundance is increased during elevated temperatures, high salt concentration, or altered pH. Under such stressful conditions, HPSs bind to proteins thereby providing protection from misfolding and aggregation. HSPs are named according to their molecular weights. Some of the most widely studied HSPs are HSP60, HSP70 and HSP90 with a molecular mass of 60, 70 and 90 kDa respectively. HSP90 is known to stabilize tumor specific proteins required for tumor growth and thus its inhibitors are being investigated as potential therapeutic targets. BioVision's Heat Shock Protein Assay Kit is a simple plate based assay that measures the activity of an enzyme in its native state and after being subjected to heat stress at 45ºC in the presence and absence of an HSP. Protective effect of the HSP is expressed as the % activity of the enzyme heated in the presence of HSP as compared to the activity of the native enzyme.
Figure: Percentage Relative Activity of enzyme subjected to heat stress in the presence of HSP70.
For more information on this kit, visit: https://www.biovision.com/heat-shock-protein-assay-kit-fluorometric.html