P23 Inhibitors
The class of P23 inhibitors comprises a diverse array of chemical compounds strategically designed to modulate cellular processes and signaling pathways, leading to the effective inhibition or modulation of P23. Geldanamycin and its derivative, 17-AAG, act as competitive inhibitors by binding to the ATP-binding site of P23, disrupting its molecular chaperone activity and compromising the folding and stability of client proteins. Quercetin and EGCG indirectly inhibit P23 by interfering with the Hsp90-P23 complex, affecting the proper functioning of P23 in cellular processes.
Radicicol, PU-H71, KRIBB11, and Novobiocin also act as competitive inhibitors, disrupting the ATP-binding site of P23 or interfering with the Hsp90-P23 complex, resulting in the destabilization and degradation of P23-associated client proteins. NVP-AUY922, KU-32-133, Withaferin A, and BIIB021 exhibit inhibitory effects by disrupting the Hsp90-P23 complex, leading to impaired chaperone activity and affecting the folding and stability of client proteins. These inhibitors collectively demonstrate the intricate strategies employed to modulate P23 activity, providing a foundation for the development of targeted interventions aimed at attenuating P23 function in diverse cellular contexts. The specificity of each inhibitor's mechanism of action highlights the potential for nuanced control over P23, opening avenues for further research into the regulatory networks governing this essential molecular chaperone.
| 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 inhibits P23 by binding to its ATP-binding site, disrupting its function as a molecular chaperone. This disruption prevents proper folding and stability of client proteins. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
17-AAG is a derivative of Geldanamycin and inhibits P23 similarly by interfering with its chaperone activity, leading to the degradation of client proteins involved in cellular processes. | ||||||
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 indirectly inhibits P23 by interfering with Hsp90, a protein complex that includes P23. This disruption affects the stability and function of P23 in chaperoning client proteins. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
EGCG is known to inhibit P23 by disrupting the Hsp90-P23 complex, leading to impaired chaperone activity. This interference results in the destabilization and degradation of client proteins. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Radicicol acts as a competitive inhibitor of P23 by binding to its ATP-binding site. This binding prevents ATP hydrolysis, disrupting the chaperone function of P23 and affecting client protein stability. | ||||||
KRIBB11 | 342639-96-7 | sc-507391 | 5 mg | $95.00 | ||
KRIBB11 inhibits P23 by disrupting the interaction between P23 and Hsp90. This disruption leads to impaired chaperone activity, affecting the folding and stability of client proteins involved in various cellular functions. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $128.00 $380.00 | ||
Novobiocin inhibits P23 by binding to its ATP-binding site, preventing ATP hydrolysis. This interference disrupts the chaperone function of P23, leading to the destabilization and degradation of client proteins. | ||||||
NVP-AUY922 | 747412-49-3 | sc-364551 sc-364551A sc-364551B sc-364551C sc-364551D sc-364551E | 5 mg 25 mg 100 mg 250 mg 1 g 5 g | $150.00 $263.00 $726.00 $1400.00 $2900.00 $11000.00 | 3 | |
NVP-AUY922 inhibits P23 by disrupting the Hsp90-P23 complex. This disruption results in the destabilization and degradation of client proteins that rely on the chaperone activity of P23 for proper folding and function. | ||||||
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 inhibits P23 by disrupting the Hsp90-P23 complex, affecting the chaperone activity of P23 and leading to the destabilization and degradation of client proteins involved in cellular functions. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
BIIB021 inhibits P23 by disrupting the Hsp90-P23 complex, resulting in impaired chaperone activity. This interference affects the folding and stability of client proteins involved in various cellular processes. | ||||||