The inhibitors targeting the functional activity of Cdc37L1 exert their biochemical effects through discrete mechanisms that impede the protein's role within specific signaling pathways or biological processes. A prominent strategy involves the direct disruption of the Hsp90/Cdc37L1 chaperone cycle. Several chemical compounds achieve this by binding to Hsp90, a molecular chaperone that Cdc37L1 associates with to facilitate the maturation of kinase clients. Inhibition of Hsp90 by these compounds results in a downstream inhibition of Cdc37L1, as its co-chaperone function is dependent on the integrity and activity of Hsp90. This consequently leads to the destabilization of kinase clients that require Cdc37L1 for folding and activation, effectively decreasing the functional activity of the protein. The specificity of these inhibitors towards Hsp90 and their subsequent effect on Cdc37L1 highlights the intricate interplay within the chaperone machinery, where the inhibition of one component can lead to the functional impairment of its partners.
Furthermore, other inhibitors indirectly influence Cdc37L1 activity by targeting similar kinases that interact with Cdc37L1 or by modulating the broader molecular environment that governs Cdc37L1's activity. Some compounds may exert their inhibitory effects by competing with Cdc37L1 for interaction with client proteins, thereby interfering with Cdc37L1's ability to perform its chaperone function effectively. Other inhibitors may allosterically affect Hsp90, which, despite not directly binding to Cdc37L1, still impairs the ability of Cdc37L1 to stabilize and activate kinase clients due to the altered functionality of the Hsp90/Cdc37L1 complex.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Staurosporine | 62996-74-1 | sc-3510 sc-3510A sc-3510B | 100 µg 1 mg 5 mg | $82.00 $150.00 $388.00 | 113 | |
A potent kinase inhibitor that disrupts multiple signaling pathways, one of which is the Hsp90/Cdc37 chaperone cycle upon which Cdc37L1 function depends, leading to the inhibition of its client protein maturation and activity. | ||||||
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $38.00 $58.00 $102.00 $202.00 | 8 | |
Specifically binds to Hsp90, inhibiting its activity. Since Cdc37L1 functions as a co-chaperone with Hsp90, this disruption inhibits the chaperoning activity of Cdc37L1, preventing proper folding and function of kinase clients. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $66.00 $153.00 | 16 | |
An analog of geldanamycin that binds to Hsp90, blocking its chaperone function. This, in turn, inhibits the Cdc37L1-co-chaperone activity, affecting the stability and activity of kinase clients. | ||||||
Silybin | 22888-70-6 | sc-202812 sc-202812A sc-202812B sc-202812C | 1 g 5 g 10 g 50 g | $54.00 $112.00 $202.00 $700.00 | 6 | |
Exhibits inhibition on the protein kinase Cdc37, which has a role similar to Cdc37L1. This could indirectly inhibit Cdc37L1 by competing for client proteins or affecting overall chaperone function. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $155.00 | 6 | |
Targets the Hsp90 chaperone complex, leading to decreased activity. The inhibition of Hsp90 affects Cdc37L1's role in the chaperone complex, hindering its function in kinase client stabilization. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $127.00 $572.00 $4090.00 $20104.00 | 20 | |
Disrupts Hsp90/Cdc37 chaperone interactions, leading to the destabilization of client proteins. This disruption can indirectly inhibit Cdc37L1 by impairing its co-chaperone function. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $96.00 $355.00 | ||
Allosterically modulates Hsp90, affecting its chaperone activity. Since Cdc37L1 acts as a co-chaperone with Hsp90, the modulation of Hsp90 activity by novobiocin can lead to the inhibition of Cdc37L1’s function. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $90.00 $326.00 | 13 | |
Binds to Hsp90, inhibiting its function. This affects the Hsp90/Cdc37L1 chaperone complex, thereby inhibiting the folding and activity of kinase clients dependent on Cdc37L1. | ||||||
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 | |
An Hsp90 inhibitor that compromises its chaperone function. This inhibits the co-chaperone activity of Cdc37L1, leading to the degradation of kinase clients. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
A synthetic inhibitor of Hsp90, which by inhibiting Hsp90, indirectly affects Cdc37L1's co-chaperone activity, thereby inhibiting associated kinase client activity. | ||||||