TMX3 Inhibitors
Chemical inhibitors of TMX3 function through various mechanisms to disrupt the protein's role in the endoplasmic reticulum (ER). Tunicamycin inhibits the initial steps of N-linked glycosylation, a process essential for the proper folding and function of many ER proteins, including TMX3, by blocking the formation of dolichol-linked oligosaccharides. Consequently, this inhibition can impair TMX3's ability to properly fold and mature glycoproteins. Brefeldin A targets ER to Golgi trafficking by inhibiting the ADP-ribosylation factor, which is crucial for the trafficking and functional localization of ER proteins such as TMX3. The disruption of this pathway can lead to a functional blockade of TMX3, as it may become improperly localized or fail to mature. Eeyarestatin I and DBeQ both target components involved in ER-associated degradation (ERAD), with the former inhibiting the p97 ATPase and associated deubiquitinases and the latter being a selective inhibitor of p97. These inhibitors can result in the accumulation of misfolded proteins, which in turn can overload TMX3's folding capacity within the ER.
Further disrupting TMX3's chaperone activity are chemicals that interfere with the ER's calcium homeostasis. Cyclopiazonic Acid and Thapsigargin both inhibit the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase (SERCA), leading to altered calcium levels, which can severely impact TMX3's folding environment. Ruthenium Red and BAPTA, by blocking calcium channels and chelating intracellular calcium respectively, also disrupt the calcium-dependent functions of TMX3. MG132 introduces stress to the ER by inhibiting proteasomes, which leads to protein accumulation and can overwhelm the protein folding machinery, including TMX3's activity. E-64's inhibition of cysteine proteases indirectly affects TMX3 by contributing to ER stress, which impedes the protein's folding environment. Lastly, Ceapin-A7 and Exo1 indirectly inhibit TMX3 by affecting upstream processes; Ceapin-A7 inhibits ATF6α signaling, a key regulator of the ER stress response, and Exo1 disrupts the ER export of specific proteins, potentially leading to an environment that challenges TMX3's protein folding capacity.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation by blocking the formation of dolichol-linked oligosaccharides. TMX3, as a protein disulfide isomerase, is involved in the folding and maturation of glycoproteins. Inhibition of glycosylation can therefore inhibit TMX3 functionality. | ||||||
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $30.00 $52.00 $122.00 $367.00 | 25 | |
Brefeldin A disrupts ER to Golgi trafficking by inhibiting ADP-ribosylation factor. TMX3, located in the ER, requires proper trafficking for function. Disruption of this trafficking can lead to functional inhibition of TMX3 by preventing its proper localization and maturation. | ||||||
Eeyarestatin I | 412960-54-4 | sc-358130B sc-358130 sc-358130A sc-358130C sc-358130D sc-358130E | 5 mg 10 mg 25 mg 50 mg 100 mg 500 mg | $112.00 $199.00 $347.00 $683.00 $1336.00 $5722.00 | 12 | |
Eeyarestatin I interferes with ER-associated degradation (ERAD) by inhibiting the p97 ATPase and associated deubiquitinases. Since TMX3 is involved in protein folding within the ER, inhibition of ERAD can lead to accumulation of misfolded proteins, thereby inhibiting TMX3's function. | ||||||
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 | |
MG132 inhibits proteasomes, which can lead to the accumulation of misfolded or unfolded proteins in the ER, causing ER stress. TMX3, which assists in protein folding in the ER, can be functionally inhibited by the increased demand and stress on the ER folding machinery. | ||||||
E-64 | 66701-25-5 | sc-201276 sc-201276A sc-201276B | 5 mg 25 mg 250 mg | $275.00 $928.00 $1543.00 | 14 | |
E-64 irreversibly inhibits cysteine proteases. TMX3's thiol-disulfide exchange activity can be indirectly inhibited if cysteine proteases that rely on proper protein folding become inhibited, leading to ER stress and disruption of TMX3's protein folding environment. | ||||||
Cyclopiazonic Acid | 18172-33-3 | sc-201510 sc-201510A | 10 mg 50 mg | $173.00 $612.00 | 3 | |
Cyclopiazonic Acid inhibits the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase (SERCA), disrupting calcium homeostasis. TMX3, being sensitive to Ca2+ levels due to its role in protein folding within the ER, can be functionally inhibited by altered Ca2+ concentrations. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin is a SERCA pump inhibitor, leading to increased cytosolic calcium levels. Elevated cytosolic calcium disrupts ER functions, therefore inhibiting TMX3's activity as it relies on a tightly regulated calcium environment for its protein folding and chaperone activity. | ||||||
Ruthenium red | 11103-72-3 | sc-202328 sc-202328A | 500 mg 1 g | $184.00 $245.00 | 13 | |
Ruthenium Red blocks calcium channels, including those located on the ER membrane. By preventing calcium influx, it can disrupt the calcium-dependent chaperone activity of TMX3 in the ER, thereby inhibiting its function in protein folding. | ||||||
BAPTA, Free Acid | 85233-19-8 | sc-201508 sc-201508A | 100 mg 500 mg | $67.00 $262.00 | 10 | |
BAPTA is a calcium chelator that can sequester intracellular calcium. The reduction in available calcium can inhibit TMX3's function, as it relies on calcium for its chaperone activity in protein folding within the ER. | ||||||
DBeQ | 177355-84-9 | sc-499943 | 10 mg | $330.00 | 1 | |
DBeQ is a selective p97 ATPase inhibitor. By inhibiting p97, it impairs the ER-associated degradation pathway, which can cause ER stress and potentially inhibit TMX3's function in assisting the folding of nascent proteins within the ER. | ||||||