Bag-5 Inhibitors
The chemical class termed BAG-5 inhibitors encompasses compounds that indirectly affect BAG-5 function by modulating the activity of heat shock proteins (HSPs) and related stress response pathways. BAG-5 is known to interact with HSPs, such as Hsp70/Hsc70, which are involved in the correct folding and prevention of aggregation of cellular proteins. Compounds that can modulate the expression or function of HSPs, therefore, have the capacity to indirectly influence the functional role of BAG-5 within the cell.
The modulation can be achieved through various mechanisms, including the induction or inhibition of heat shock responses, binding to HSPs to prevent their interaction with client proteins or co-chaperones, and altering the stability and expression of these proteins. These chemical agents, while not directly interacting with BAG-5, alter the cellular milieu in which BAG-5 operates, thereby affecting its role in cellular protein homeostasis. Through these mechanisms, these agents exert an indirect effect on BAG-5, influencing processes ranging from protein folding to cellular stress responses. The result is a change in the functional dynamics of BAG-5 within the cell, impacting its co-chaperone activity and the regulation of associated proteins.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 Hsp90, potentially altering its interaction with BAG-5, which in turn might influence the chaperone's activity and client protein handling. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
Similar to Geldanamycin, 17-AAG interferes with Hsp90’s function, which can affect BAG-5-related pathways by modulating stress responses and protein folding. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $158.00 | 6 | |
Celastrol induces heat shock response and can modulate the activity of heat shock proteins that are known to associate with BAG-5, thereby affecting its function. | ||||||
Heat Shock Protein Inhibitor I | 218924-25-5 | sc-221709 | 5 mg | $97.00 | 5 | |
Heat Shock Protein Inhibitor I, KNK437, is a heat shock protein inhibitor, which can lead to the reduced activity of Hsp70, thereby potentially affecting BAG-5's regulatory functions. | ||||||
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 has been shown to interfere with the expression of heat shock proteins, which could indirectly modulate BAG-5's role in protein homeostasis. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $90.00 $204.00 | 13 | |
Triptolide has been observed to disrupt heat shock responses, possibly affecting BAG-5's function due to its interaction with heat shock proteins. | ||||||
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 can lead to increased cellular stress, potentially impacting the BAG-5-associated stress response pathways. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $130.00 $583.00 $4172.00 $20506.00 | 20 | |
Withaferin A disrupts the function of Hsp90, which could affect the associated regulatory proteins like BAG-5 by altering their stability and function. | ||||||
Pifithrin-α hydrobromide | 63208-82-2 | sc-45050 sc-45050A | 5 mg 25 mg | $120.00 $300.00 | 36 | |
Pifithrin-α(HBr) inhibits Hsp70, which may affect its co-chaperone BAG-5, impacting the stability and folding of various proteins within the cell. | ||||||
Zerumbone | 471-05-6 | sc-364148 sc-364148A | 10 mg 50 mg | $112.00 $408.00 | ||
Zerumbone has been reported to modulate heat shock protein expression, which may influence BAG-5 function indirectly through its role in protein folding. | ||||||