HSPB3 Inhibitors
HSPB3 inhibitors are a class of small molecules that target and modulate the function of Heat Shock Protein Beta-3 (HSPB3), which belongs to the small heat shock protein (sHSP) family. These proteins are known for their role in chaperoning cellular proteins under stress conditions and maintaining cellular homeostasis by preventing aggregation of unfolded proteins. HSPB3, specifically, is one of the less studied sHSPs, and it has been associated with the stabilization of intermediate filaments and cytoskeletal integrity. Structurally, HSPB3 contains a conserved α-crystallin domain typical of sHSPs, facilitating its oligomerization and interaction with other protein partners. Inhibitors targeting HSPB3 are designed to disrupt these interactions, altering its ability to function as a chaperone. These inhibitors are typically developed to understand the biological functions of HSPB3 by perturbing its activity and assessing downstream effects in various cellular contexts.
The chemical structure of HSPB3 inhibitors varies widely, but they often share features common to small molecule inhibitors of other sHSPs, such as hydrophobic moieties that allow binding within the α-crystallin domain, and regions that enable selective binding to HSPB3 over other sHSP family members. The specificity of these inhibitors is particularly important for dissecting the unique cellular roles of HSPB3, given its distinct expression pattern and functions compared to other sHSPs. The impact of HSPB3 inhibition can span several cellular processes, including protein folding, cytoskeletal organization, and stress responses, allowing researchers to gain insights into how this protein modulates cellular dynamics. By manipulating the activity of HSPB3 with selective inhibitors, studies can elucidate the contributions of HSPB3 to cellular physiology and explore its role in diverse biological processes.
SEE ALSO...
Items 1 to 10 of 11 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
Binds specifically to the ATPase domain of heat shock protein 90 (HSP90). Inhibition of HSP90 leads to the destabilization of its client proteins, including HSPB3, by preventing proper folding and promoting proteasomal degradation. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
Inhibits HSP90 activity. It blocks the maturation of proteins that depend on HSP90 for conformational stabilization, thus indirectly leading to the functional inhibition of HSPB3 through increased degradation of misfolded HSPB3. | ||||||
17-DMAG | 467214-20-6 | sc-202005 | 1 mg | $205.00 | 8 | |
Binds to HSP90, inhibiting its chaperone activity. This prevents proper folding of HSPB3, resulting in its degradation and decreased functional activity. | ||||||
Silybin | 22888-70-6 | sc-202812 sc-202812A sc-202812B sc-202812C | 1 g 5 g 10 g 50 g | $55.00 $114.00 $206.00 $714.00 | 6 | |
Known to inhibit the expression of HSP70, a chaperone protein closely related to the HSPB family. This inhibition can lead to an indirect reduction in HSPB3 activity due to the integrated stress response within the cell. | ||||||
AT13387 | 912999-49-6 | sc-364415 sc-364415A | 10 mg 50 mg | $555.00 $1606.00 | ||
Is an HSP90 inhibitor that binds to its N-terminal domain, preventing the chaperone cycle required for the maturation of its client proteins. This results in the degradation of associated proteins such as HSPB3. | ||||||
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 | |
Is a potent inhibitor of HSP90, causing the degradation of client proteins that rely on HSP90 for proper folding. This leads to the indirect inhibition of HSPB3 by increasing its misfolded and degraded forms. | ||||||
Ganetespib | 888216-25-9 | sc-364496 sc-364496A | 10 mg 250 mg | $273.00 $1040.00 | ||
Binds to the ATP-binding domain of HSP90, hindering its activity. The compromised chaperone function results in the destabilization and degradation of its client proteins, including HSPB3. | ||||||
Phenethyl isothiocyanate | 2257-09-2 | sc-205801 sc-205801A | 5 g 10 g | $104.00 $183.00 | 2 | |
Is known to modulate heat shock proteins and can decrease the expression of HSP70. This can indirectly lead to a decrease in HSPB3 activity due to the interconnected nature of heat shock protein response. | ||||||
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 $110.00 $250.00 $936.00 $50.00 | 33 | |
Has been found to modulate HSP expression. It can downregulate HSP70, which may in turn affect HSPB3 function indirectly by altering the heat shock protein response and possibly reducing the stability of HSPB3. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $90.00 $204.00 | 13 | |
Has been shown to downregulate heat shock proteins, including HSP70. HSPB3, being part of the small heat shock protein family, could be indirectly inhibited due to the impairment of the heat shock response. | ||||||