Date published: 2026-5-30

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DnaJC18 Inhibitors

DNAJC18 Inhibitors represent a distinctive chemical class characterized by their ability to modulate the function of DNAJC18, a protein critically involved in various intracellular processes. DNAJC18 is a member of the DNAJ (HSP40) family, which plays a pivotal role in protein folding, chaperone-mediated protein trafficking, and cellular protein quality control. Operating within the intricate machinery of the cell, DNAJC18 collaborates with an array of partner proteins to facilitate the correct folding of nascent polypeptides, ensuring their structural integrity and functional competence. Additionally, DNAJC18 assists in the maintenance of protein homeostasis by reducing the aggregation of misfolded proteins and facilitating their degradation. DNAJC18 Inhibitors, part of the broader landscape of molecular tools, are meticulously designed molecules that selectively bind to specific regions of the DNAJC18 protein.

This binding interaction can disrupt the normal conformational changes necessary for its functional activities. By doing so, these inhibitors have the potential to perturb the tightly regulated protein folding pathways and intricate protein-protein interactions that rely on DNAJC18's participation. This interference could subsequently cascade into disruptions in cellular protein trafficking and the accurate delivery of proteins to their designated subcellular compartments.

The design of DNAJC18 Inhibitors requires a comprehensive understanding of the protein's structure and function, enabling researchers to identify key binding sites that could be targeted by these inhibitors. These small molecules are engineered to exhibit high binding affinity and specificity for DNAJC18, minimizing off-target effects. Ongoing investigations into the molecular interactions between these inhibitors and DNAJC18 are shedding light on the underlying mechanisms of protein folding and cellular quality control. These insights could potentially have far-reaching implications for understanding cellular physiology and pathology.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Radicicol

12772-57-5sc-200620
sc-200620A
1 mg
5 mg
$92.00
$333.00
13
(1)

Binds to the ATP-binding site of Hsp90, a chaperone protein that interacts with DNAJC18, disrupting protein folding pathways.

Geldanamycin

30562-34-6sc-200617B
sc-200617C
sc-200617
sc-200617A
100 µg
500 µg
1 mg
5 mg
$39.00
$59.00
$104.00
$206.00
8
(1)

Similar to radicicol, geldanamycin binds Hsp90, leading to inhibition of DNAJC18-associated protein folding.

Novobiocin

303-81-1sc-362034
sc-362034A
5 mg
25 mg
$128.00
$380.00
(0)

Targets the DNAJC18-Hsp90 complex by binding to its ATPase domain, interfering with chaperone-assisted protein maturation.

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)

Acts as an ATP-competitive inhibitor of Hsp90, influencing the stability and function of DNAJC18-interacting proteins.

BIIB 021

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

Inhibits Hsp90 ATPase activity, leading to the disruption of DNAJC18-chaperone interactions and protein folding pathways.

KRIBB11

342639-96-7sc-507391
5 mg
$95.00
(0)

Blocks the interaction between DNAJC18 and Hsp70, impacting chaperone-mediated protein folding and cellular functions.

17-AAG

75747-14-7sc-200641
sc-200641A
1 mg
5 mg
$67.00
$156.00
16
(2)

Binds to Hsp90, including its DNAJC18-associated form, leading to destabilization and degradation of client proteins.

AT13387

912999-49-6sc-364415
sc-364415A
10 mg
50 mg
$555.00
$1606.00
(0)

Inhibits Hsp90 function, including its interaction with DNAJC18, resulting in impaired protein folding and cellular effects.

IPI-504

857402-63-2sc-364512
sc-364512A
10 mg
50 mg
$640.00
$1600.00
(0)

Another Hsp90 inhibitor, retaspimycin HCl, affects DNAJC18-associated chaperone machinery and protein folding processes.