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.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Binds to the ATP-binding site of Hsp90, a chaperone protein that interacts with DNAJC18, disrupting protein folding pathways. | ||||||
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 | |
Similar to radicicol, geldanamycin binds Hsp90, leading to inhibition of DNAJC18-associated protein folding. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $128.00 $380.00 | ||
Targets the DNAJC18-Hsp90 complex by binding to its ATPase domain, interfering with chaperone-assisted protein maturation. | ||||||
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 | |
Acts as an ATP-competitive inhibitor of Hsp90, influencing the stability and function of DNAJC18-interacting proteins. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
Inhibits Hsp90 ATPase activity, leading to the disruption of DNAJC18-chaperone interactions and protein folding pathways. | ||||||
KRIBB11 | 342639-96-7 | sc-507391 | 5 mg | $95.00 | ||
Blocks the interaction between DNAJC18 and Hsp70, impacting chaperone-mediated protein folding and cellular functions. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
Binds to Hsp90, including its DNAJC18-associated form, leading to destabilization and degradation of client proteins. | ||||||
AT13387 | 912999-49-6 | sc-364415 sc-364415A | 10 mg 50 mg | $555.00 $1606.00 | ||
Inhibits Hsp90 function, including its interaction with DNAJC18, resulting in impaired protein folding and cellular effects. | ||||||
IPI-504 | 857402-63-2 | sc-364512 sc-364512A | 10 mg 50 mg | $640.00 $1600.00 | ||
Another Hsp90 inhibitor, retaspimycin HCl, affects DNAJC18-associated chaperone machinery and protein folding processes. | ||||||