PTGES3L-AARSD1 Inhibitors
Chemical inhibitors of PTGES3L-AARSD1 can disrupt its function through a variety of mechanisms, primarily by interfering with the protein folding and degradation pathways within the cell. Trichostatin A, as a histone deacetylase inhibitor, can affect the acetylation state of histones, which in turn impacts the chaperone activity of PTGES3L-AARSD1. This is due to the fact that histone modification can influence the protein folding environment, potentially leading to an inhibition of the chaperone-like functions of PTGES3L-AARSD1. Similarly, geldanamycin and its analog 17-AAG, target the chaperone protein Hsp90, compromising its function. Since PTGES3L-AARSD1 is suggested to have a chaperone-like domain, the inhibition of Hsp90 can destabilize client proteins and disrupt the protein folding process that PTGES3L-AARSD1 may be involved in. Withaferin A and celastrol both inhibit the proteasome, which can lead to the accumulation of misfolded proteins, thus overwhelming the cellular protein folding machinery and indirectly inhibiting the function of PTGES3L-AARSD1.
Further compounding the stress on PTGES3L-AARSD1's chaperone-like activity, MG-132 and epoxomicin, both proteasome inhibitors, cause an accumulation of ubiquitinated proteins, which can disturb cellular proteostasis. This can overload PTGES3L-AARSD1's capacity to deal with misfolded proteins. Bortezomib, another proteasome inhibitor, impairs the degradation pathway of misfolded proteins, which can result in an increased load on PTGES3L-AARSD1. Concanamycin A disrupts protein trafficking by inhibiting V-ATPase, leading to an increase in misfolded proteins which may inhibit PTGES3L-AARSD1 indirectly. Lactacystin, like other proteasome inhibitors, also contributes to the functional inhibition of PTGES3L-AARSD1 by preventing the degradation of misfolded proteins. Lastly, puromycin disrupts protein synthesis, which can lead to an increased burden on the protein folding machinery of the cell, including PTGES3L-AARSD1, by causing an accumulation of proteins that have not been properly synthesized and folded.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Trichostatin A | 58880-19-6 | sc-3511 sc-3511A sc-3511B sc-3511C sc-3511D | 1 mg 5 mg 10 mg 25 mg 50 mg | $149.00 $470.00 $620.00 $1199.00 $2090.00 | 33 | |
Trichostatin A is known as a histone deacetylase inhibitor, and by altering the acetylation state of histones, it can impact the chaperone activity of PTGES3L-AARSD1, as histone modification can affect the folding environment of various proteins including PTGES3L-AARSD1. | ||||||
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 binds to Hsp90 and inhibits its chaperone function. Given that PTGES3L-AARSD1 has a chaperone-like domain, the inhibition of Hsp90 can disrupt the folding and stability of proteins that rely on the Hsp90 complex, including potential clients like PTGES3L-AARSD1. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $66.00 $153.00 | 16 | |
17-AAG, an analog of Geldanamycin, also targets Hsp90 and impairs its activity. The inhibition of Hsp90 may destabilize proteins associated with the chaperone complex, potentially leading to the reduced functionality of PTGES3L-AARSD1 if it is a client protein. | ||||||
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 has been shown to inhibit the proteasome, which could lead to the accumulation of misfolded proteins and affect the protein folding environment in the cell, thereby potentially inhibiting the function of PTGES3L-AARSD1 by overwhelming its chaperone-like activity. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $155.00 | 6 | |
Celastrol is a known inhibitor of the proteasome and can induce heat shock response. By inhibiting the proteasome, it can indirectly affect the chaperone network within the cell, potentially disrupting the function of PTGES3L-AARSD1 by altering its substrate protein folding landscape. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $56.00 $260.00 $980.00 | 163 | |
MG-132 is a proteasome inhibitor that can lead to the accumulation of ubiquitinated proteins and may disturb the cellular protein homeostasis, which could impair the function of chaperone-like proteins such as PTGES3L-AARSD1 by overloading the protein quality control system. | ||||||
Epoxomicin | 134381-21-8 | sc-201298C sc-201298 sc-201298A sc-201298B | 50 µg 100 µg 250 µg 500 µg | $134.00 $215.00 $440.00 $496.00 | 19 | |
Epoxomicin is a selective proteasome inhibitor, which through the accumulation of polyubiquitinated proteins, may indirectly inhibit chaperone proteins like PTGES3L-AARSD1 by disrupting the normal proteostasis and chaperone-assisted folding process. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
Bortezomib is a dipeptide boronic acid and a proteasome inhibitor. By inhibiting the proteasome, the degradation pathway of misfolded proteins is impaired, which could lead to a functional inhibition of PTGES3L-AARSD1 by increasing its client protein load beyond capacity. | ||||||
Concanamycin A | 80890-47-7 | sc-202111 sc-202111A sc-202111B sc-202111C | 50 µg 200 µg 1 mg 5 mg | $65.00 $162.00 $650.00 $2550.00 | 109 | |
Concanamycin A is a specific inhibitor of V-ATPase, which can alter endosomal-lysosomal pH and disrupt protein trafficking. Disruption of protein trafficking could lead to an increase in misfolded protein levels, potentially inhibiting the chaperone function of PTGES3L-AARSD1. | ||||||
Lactacystin | 133343-34-7 | sc-3575 sc-3575A | 200 µg 1 mg | $165.00 $575.00 | 60 | |
Lactacystin is a specific inhibitor of the proteasome. By inhibiting the proteasome, the degradation of misfolded proteins is impaired, potentially resulting in an overload of the chaperone systems, including PTGES3L-AARSD1, leading to its functional inhibition. | ||||||