Date published: 2025-11-24

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Cdc37L1 Inhibitors

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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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Staurosporine

62996-74-1sc-3510
sc-3510A
sc-3510B
100 µg
1 mg
5 mg
$82.00
$150.00
$388.00
113
(4)

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

30562-34-6sc-200617B
sc-200617C
sc-200617
sc-200617A
100 µg
500 µg
1 mg
5 mg
$38.00
$58.00
$102.00
$202.00
8
(1)

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

75747-14-7sc-200641
sc-200641A
1 mg
5 mg
$66.00
$153.00
16
(2)

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

22888-70-6sc-202812
sc-202812A
sc-202812B
sc-202812C
1 g
5 g
10 g
50 g
$54.00
$112.00
$202.00
$700.00
6
(1)

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

34157-83-0sc-202534
10 mg
$155.00
6
(1)

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

5119-48-2sc-200381
sc-200381A
sc-200381B
sc-200381C
1 mg
10 mg
100 mg
1 g
$127.00
$572.00
$4090.00
$20104.00
20
(1)

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

303-81-1sc-362034
sc-362034A
5 mg
25 mg
$96.00
$355.00
(0)

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

12772-57-5sc-200620
sc-200620A
1 mg
5 mg
$90.00
$326.00
13
(1)

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

747412-49-3sc-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
(1)

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

848695-25-0sc-364434
sc-364434A
5 mg
25 mg
$128.00
$650.00
(0)

A synthetic inhibitor of Hsp90, which by inhibiting Hsp90, indirectly affects Cdc37L1's co-chaperone activity, thereby inhibiting associated kinase client activity.