Chemical activators of Heat Shock Factor 3 (HSF3) can induce a cellular response through various mechanisms of molecular stress. Celastrol, for instance, instigates the activation of HSF3 by promoting the misfolding of proteins within the cell, which necessitates the defensive expression of heat shock proteins (HSPs) to mitigate this stress. This response is a vital aspect of the cell's mechanism to maintain proteostasis. Another compound, Geldanamycin, operates by binding to and inhibiting Heat Shock Protein 90 (Hsp90), a chaperone protein that typically represses HSF3. When Hsp90 is inhibited, HSF3 is released and becomes active, initiating the heat shock response. Similarly, 17-AAG, a derivative of Geldanamycin, suppresses Hsp90 activity, leading to the activation of HSF3 and the promotion of the heat shock protein response. Sodium Arsenite and Cadmium Chloride act as activators of HSF3 by causing protein denaturation, which signals the cell to produce heat shock proteins as a protective measure.
Other substances such as MG-132 and Bortezomib, both proteasome inhibitors, lead to the accumulation of ubiquitinated proteins. This accumulation triggers cellular stress and consequently the activation of HSF3, as the cell attempts to handle and dispose of the misfolded or damaged proteins. Zinc Chloride activates HSF3 by inducing oxidative stress, which requires a cellular defense mechanism to ensure correct protein folding and function. Quercetin, a naturally occurring flavonoid, is thought to activate HSF3 by stabilizing it in its active state, thereby facilitating the expression of heat shock proteins. Triptolide and Withaferin A induce cellular stress, which leads to the activation of HSF3 and the upregulation of HSPs to protect against protein misfolding and damage. Lastly, Emetine activates HSF3 through the induction of ribotoxic stress, highlighting the cellular necessity to manage the unfolded protein response, promoting the functional activation of HSF3 for the upregulation of heat shock proteins.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $158.00 | 6 | |
Celastrol activates heat shock transcription factor 3 (HSF3) by inducing cellular stress responses. This triterpenoid compound causes the misfolding of proteins, which in turn activates HSF3 as a defense mechanism to initiate the expression of heat shock proteins (HSPs) to counteract the stress, resulting in the functional activation of HSF3 to maintain proteostasis. | ||||||
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $39.00 $59.00 $104.00 $206.00 | 8 | |
Geldanamycin binds to and inhibits Hsp90, a chaperone protein that normally represses HSF3. The inhibition of Hsp90 leads to the release and activation of HSF3, which then undergoes trimerization and translocates to the nucleus to drive the heat shock response, thus functionally activating HSF3. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
17-AAG, a derivative of geldanamycin, similarly inhibits Hsp90 activity. This disruption of Hsp90 function results in the liberation and activation of HSF3, enabling it to perform its role in the heat shock protein response. | ||||||
Sodium arsenite, 0.1N Standardized Solution | 7784-46-5 | sc-301816 | 500 ml | $130.00 | 4 | |
Sodium Arsenite induces heat shock protein synthesis by causing the denaturation of proteins, which activates HSF3. The activation of HSF3 occurs to enhance the cellular capacity to refold or degrade the misfolded proteins, which is a protective cellular mechanism against stress. | ||||||
Cadmium chloride, anhydrous | 10108-64-2 | sc-252533 sc-252533A sc-252533B | 10 g 50 g 500 g | $56.00 $183.00 $352.00 | 1 | |
Cadmium Chloride is a heavy metal that induces protein misfolding, thus activating HSF3. The activation of HSF3 facilitates the cellular response to the stress of misfolded proteins by upregulating heat shock proteins that assist in refolding and preventing aggregation. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $60.00 $265.00 $1000.00 | 163 | |
MG-132 is a proteasome inhibitor that leads to the accumulation of ubiquitinated proteins, causing cellular stress and the consequent activation of HSF3 as part of the cellular attempt to manage the misfolded or damaged proteins. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $135.00 $1085.00 | 115 | |
Bortezomib, another proteasome inhibitor, similarly causes an accumulation of misfolded proteins, which activates HSF3. The activation of HSF3 triggers an increase in the heat shock protein response to help alleviate the proteotoxic stress. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc Chloride can induce oxidative stress, which in turn activates HSF3. The activation of HSF3 is part of the cellular defense mechanism against oxidative damage and to ensure proper protein folding and function. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $110.00 $250.00 $936.00 $50.00 | 33 | |
Quercetin, a flavonoid, can induce the heat shock response by activating HSF3. It is thought to do so by stabilizing HSF3 in its active form, allowing it to promote the expression of heat shock proteins. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $90.00 $204.00 | 13 | |
Triptolide can induce a heat shock response by activating HSF3. This activation likely occurs through the induction of cellular stress, which necessitates the upregulation of HSPs to protect against protein misfolding and damage. | ||||||