DnaJB3 inhibitors are a class of chemical compounds designed to inhibit the activity of the DnaJB3 protein, a member of the Hsp40 family of heat shock proteins, also known as J-domain proteins. DnaJB3 plays a key role in protein folding and quality control within the cell, primarily by acting as a co-chaperone with Hsp70. It helps in the regulation of protein homeostasis by binding to misfolded or aggregated proteins, facilitating their proper folding or directing them toward degradation pathways. DnaJB3 is critical in maintaining the stability of proteins, especially under conditions of cellular stress, where the demand for protein quality control is heightened. By inhibiting DnaJB3, these compounds disrupt its co-chaperone function, potentially affecting the protein folding machinery and increasing the accumulation of misfolded proteins.
Chemically, DnaJB3 inhibitors are typically designed to interact with the protein's J-domain, the region responsible for stimulating the ATPase activity of Hsp70, or with other functional domains that are essential for its co-chaperone activity. These inhibitors may work by preventing DnaJB3 from interacting with Hsp70 or by blocking its ability to bind substrate proteins. This disruption in the DnaJB3-Hsp70 complex can lead to alterations in protein folding pathways, affecting the overall balance of protein quality control within cells. The study of DnaJB3 inhibitors is valuable for understanding the complex mechanisms of molecular chaperones and their role in maintaining cellular protein homeostasis. Additionally, this research helps elucidate the importance of J-domain proteins in regulating protein folding, degradation, and stress response, offering insights into how cells manage proteotoxic stress and maintain functional proteomes.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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VER 155008 | 1134156-31-2 | sc-358808 sc-358808A | 10 mg 50 mg | $199.00 $825.00 | 9 | |
VER-155008, a HSP70 inhibitor, indirectly inhibits DNAJB3 by disrupting the interaction with HSP70, reducing the co-chaperone activity and hindering protein folding efficiency, consequently impacting cellular stress responses. | ||||||
JG-98 | 1456551-16-8 | sc-507517 | 5 mg | $220.00 | ||
JG-98, a small molecule inhibitor, directly targets DNAJB3, impeding its co-chaperone activity and limiting its collaboration with HSP70, thereby compromising the protein folding process and cellular stress response. | ||||||
Myricetin | 529-44-2 | sc-203147 sc-203147A sc-203147B sc-203147C sc-203147D | 25 mg 100 mg 1 g 25 g 100 g | $95.00 $184.00 $255.00 $500.00 $1002.00 | 3 | |
Myricetin, a flavonoid, indirectly influences DNAJB3 by modulating MAPK signaling, potentially affecting its co-chaperone activity and cellular stress response, offering an avenue for the regulation of protein folding efficiency under stress conditions. | ||||||
Pifithrin-μ | 64984-31-2 | sc-203195 sc-203195A | 10 mg 50 mg | $127.00 $372.00 | 4 | |
Pifithrin-μ, a p53 inhibitor, indirectly influences DNAJB3 by impacting the p53 pathway, potentially affecting its co-chaperone activity and cellular stress response, suggesting a link between DNAJB3 regulation and cellular responses to stressors. | ||||||
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 | |
Withaferin A, a natural compound, indirectly influences DNAJB3 by modulating NF-κB signaling, potentially impacting its co-chaperone activity and cellular stress response, providing insights into the regulation of protein folding efficiency in response to various stressors. | ||||||
17-DMAG, Hydrochloride Salt | 467214-21-7 | sc-396751 | 25 mg | $306.00 | ||
17-DMAG, a HSP90 inhibitor, indirectly influences DNAJB3 by disrupting the HSP90-DNAJB3 interaction, potentially affecting its co-chaperone activity and cellular stress response, revealing a connection between HSP90 inhibition and the modulation of DNAJB3 function. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $88.00 $200.00 | 13 | |
Triptolide, a natural product, indirectly influences DNAJB3 by modulating JNK signaling, potentially impacting its co-chaperone activity and cellular stress response, highlighting a potential regulatory mechanism for protein folding efficiency under stress conditions. | ||||||
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 $108.00 $245.00 $918.00 $49.00 | 33 | |
Quercetin, a flavonoid, indirectly influences DNAJB3 by modulating AMPK signaling, potentially affecting its co-chaperone activity and cellular stress response, providing insights into the regulation of protein folding efficiency in response to various stressors. | ||||||
2-Deoxy-D-glucose | 154-17-6 | sc-202010 sc-202010A | 1 g 5 g | $65.00 $210.00 | 26 | |
2-Deoxyglucose, a glycolytic inhibitor, indirectly influences DNAJB3 by modulating energy metabolism, potentially impacting its co-chaperone activity and cellular stress response, suggesting a link between cellular energy status and the regulation of DNAJB3 function. | ||||||
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 | |
Geldanamycin, a HSP90 inhibitor, indirectly influences DNAJB3 by disrupting the HSP90-DNAJB3 interaction, potentially affecting its co-chaperone activity and cellular stress response, revealing a connection between HSP90 inhibition and the modulation of DNAJB3 function. |