HSP Inhibitors
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Pifithrin-μ | 64984-31-2 | sc-203195 sc-203195A | 10 mg 50 mg | $130.00 $379.00 | 4 | |
Pifithrin-μ functions as a potent inhibitor of heat shock protein 70 (HSP70), exhibiting a unique mechanism of action through its interaction with the substrate-binding domain. This compound disrupts the chaperone-client protein interactions, leading to altered protein folding and degradation pathways. Its kinetic profile reveals a rapid association with HSP70, effectively modulating cellular stress responses and influencing the stability of misfolded proteins. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Radicicol acts as a selective inhibitor of heat shock protein 90 (HSP90), engaging with the ATP-binding pocket to disrupt its chaperone function. This interaction impedes the conformational changes necessary for client protein maturation, leading to their destabilization. The compound exhibits a unique binding affinity that alters the kinetics of HSP90's ATPase activity, ultimately affecting the cellular response to stress and protein homeostasis. | ||||||
Heat Shock Protein Inhibitor I | 218924-25-5 | sc-221709 | 5 mg | $97.00 | 5 | |
Heat Shock Protein Inhibitor I selectively targets heat shock proteins, particularly HSP70, by binding to its substrate-binding domain. This interaction disrupts the protein's ability to assist in the proper folding and stabilization of client proteins under stress conditions. The inhibitor's unique structural features enhance its specificity, modulating the chaperone cycle and influencing the degradation pathways of misfolded proteins, thereby impacting cellular stress responses and proteostasis. | ||||||
Heat Shock Protein Inhibitor II | 1859-42-3 | sc-221710 | 10 mg | $137.00 | ||
Heat Shock Protein Inhibitor II exhibits a distinct mechanism by interacting with the ATPase domain of heat shock proteins, particularly HSP90. This binding alters the conformational dynamics of the chaperone, impairing its ability to facilitate client protein maturation and stabilization. The inhibitor's unique molecular architecture promotes selective disruption of client protein interactions, thereby influencing cellular signaling pathways and stress response mechanisms, ultimately affecting protein homeostasis. | ||||||
PF-04929113 | 908115-27-5 | sc-364576 sc-364576A | 5 mg 50 mg | $495.00 $1980.00 | ||
PF-04929113 functions as a selective modulator of heat shock proteins, specifically targeting the ATP-binding site of HSP70. Its unique structural features enable it to disrupt the chaperone's interaction with substrate proteins, leading to altered folding pathways and impaired protein stabilization. This compound exhibits distinct kinetic properties, influencing the rate of client protein release and enhancing the degradation of misfolded proteins, thereby impacting cellular stress responses and proteostasis. | ||||||
VER-50589 | 747413-08-7 | sc-296692 sc-296692A | 500 µg 1 mg | $70.00 $110.00 | ||
VER-50589 acts as a selective heat shock protein modulator, engaging with HSP90 through its unique binding affinity. This compound alters the conformational dynamics of HSP90, disrupting its interaction with client proteins and affecting their maturation pathways. Its distinct molecular interactions lead to a modulation of chaperone activity, influencing the stability and turnover of key regulatory proteins, thereby impacting cellular homeostasis and stress response mechanisms. | ||||||