HSPA4L Inhibitors
HSPA4L inhibitors constitute a class of chemical compounds designed specifically to obstruct the functional activities of the HSPA4L protein. The HSPA4L protein, which is a member of the heat shock protein family, participates in cellular processes that facilitate the correct folding of nascent proteins and the repair or degradation of misfolded proteins. Inhibition of HSPA4L can disrupt these processes, potentially leading to an accumulation of misfolded proteins and the subsequent activation of cellular stress responses. HSPA4L inhibitors achieve their effects by binding to the ATPase domain of the protein, preventing ATP hydrolysis which is crucial for the protein's function. This binding impairs the protein's ability to interact with its substrates, thereby inhibiting its chaperone activity. As a result, the normal homeostatic functions that HSPA4L regulates within the cell are hampered, leading to a decrease in the cell's ability to manage proteomic stress.
The specific chemical inhibitors targeting HSPA4L are crafted to ensure high affinity and specificity to the protein's active sites. By doing so, these inhibitors can effectively modulate the stress response pathways that HSPA4L is involved in. Through the inhibition of HSPA4L, these compounds can indirectly affect various signaling pathways and molecular processes that rely on the proper functioning of chaperone-mediated protein folding. The precise mechanisms of these inhibitors involve the alteration of the conformational dynamics of HSPA4L, which in turn influences the protein's stability and its interactions with co-chaperones and client proteins. This action reflects a critical aspect of cellular regulation, as HSPA4L plays a role in the maintenance of protein homeostasis, and its inhibition can lead to a cascade of effects within the cellular environment that extend beyond the initial protein-protein interactions.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
Quercetin is a flavonoid that inhibits the heat shock protein family, which includes HSPA4L. By stabilizing HSP70, it indirectly prevents the proper functioning of HSPA4L, as HSPA4L operates within a complex with other heat shock proteins, thus diminishing HSPA4L's chaperone activity. | ||||||
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 | |
Geldanamycin binds specifically to heat shock protein 90 (Hsp90) and inhibits its function. Since HSPA4L is a co-chaperone for Hsp90, the inhibition of Hsp90 disrupts the Hsp90-HSPA4L association, thus indirectly reducing HSPA4L activity. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
17-AAG is a derivative of Geldanamycin which also binds to Hsp90. It destabilizes and degrades client proteins of Hsp90, which may include proteins that interact with HSPA4L, leading to a reduction in HSPA4L activity by association. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $130.00 $583.00 $4172.00 $20506.00 | 20 | |
Withaferin A is known for its ability to inhibit the function of Hsp90, and by extension, it is likely to disrupt HSPA4L's role as a co-chaperone, thus decreasing its activity. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Radicicol binds to Hsp90, inhibiting its ATPase activity. Since HSPA4L functions in tandem with Hsp90, inhibition of Hsp90 by Radicicol would result in decreased HSPA4L 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 | |
Silibinin has been shown to influence heat shock protein expression. It may downregulate the activity of HSPA4L by modulating the expression levels of molecular chaperones within the cell. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
EGCG, a catechin found in green tea, has been reported to modulate the heat shock response. It may hinder HSPA4L activity by affecting the overall heat shock protein response. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $90.00 $204.00 | 13 | |
Triptolide has been shown to induce heat shock protein expression. It could potentially inhibit HSPA4L by causing an imbalanced stress response, leading to a decrease in its functional activity. | ||||||
Heat Shock Protein Inhibitor I | 218924-25-5 | sc-221709 | 5 mg | $97.00 | 5 | |
KNK437 is a benzylidene lactam compound that inhibits the synthesis of heat shock proteins. This inhibition likely extends to HSPA4L, as it is a part of the heat shock protein family. | ||||||
Tryptanthrin | 13220-57-0 | sc-202844 sc-202844A | 1 mg 5 mg | $50.00 $213.00 | ||
Tryptanthrin has been identified as an inhibitor of heat shock response, which may result in decreased activity of HSPA4L through suppression of the cellular stress response. | ||||||