TXNDC10 Inhibitors
Chemical inhibitors of TXNDC10 act through various mechanisms to disrupt its role in the oxidative protein folding process within the endoplasmic reticulum (ER). Bacitracin, by inhibiting protein disulfide isomerase (PDI), hampers the formation of proper disulfide bonds crucial for protein folding, thus affecting the function of TXNDC10, which works in conjunction with PDI. Aurintricarboxylic Acid, through its inhibition of nucleases, can alter the redox state in the ER, leading to consequences for the protein-folding function of TXNDC10. Ebselen, with its glutathione peroxidase mimicking action, and by irreversibly inhibiting thioredoxin reductase, disrupts the thioredoxin system, which is closely linked to the redox regulation that TXNDC10 requires. PX-12's irreversible inhibition of thioredoxin-1 similarly leads to a disturbance in the intracellular redox environment, which can affect TXNDC10's activity.
Furthermore, ML171's inhibition of NADPH oxidase (NOX), the enzyme responsible for producing reactive oxygen species necessary for oxidative folding, can interfere with TXNDC10's functioning. Auranofin, another inhibitor of thioredoxin reductase, can alter the redox environment and indirectly affect TXNDC10's activity. Salubrinal targets eIF2α phosphatase, leading to eIF2α phosphorylation accumulation, which is part of the unfolded protein response; this can impede TXNDC10's response to misfolded proteins. Tunicamycin's inhibition of N-linked glycosylation, which is vital for proteins in the ER, can induce ER stress and indirectly inhibit TXNDC10. Brefeldin A, by disrupting ER to Golgi transport, can overwhelm TXNDC10's protein-folding capacity. Dehydroascorbic acid, by reducing glutathione levels, disrupts cellular redox balance, affecting TXNDC10. Thapsigargin, by depleting ER calcium stores necessary for chaperone function, can inhibit TXNDC10. Lastly, Disulfiram's inhibition of thiol-reliant enzymes can impact the function of TXNDC10 in the formation of disulfide bonds in proteins. Each chemical, through its distinct mechanism, can influence the normal function of TXNDC10 within the cell.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Bacitracin | 1405-87-4 | sc-252399 | 5 g | $87.00 | 1 | |
Bacitracin inhibits protein disulfide isomerase (PDI), which is essential for the formation of proper disulfide bonds in the endoplasmic reticulum. TXNDC10, as a protein that assists in protein folding in the ER, relies on PDI to function properly, so inhibition of PDI by bacitracin leads to the functional inhibition of TXNDC10. | ||||||
Aurintricarboxylic Acid | 4431-00-9 | sc-3525 sc-3525A sc-3525B sc-3525C | 100 mg 1 g 5 g 10 g | $20.00 $31.00 $47.00 $92.00 | 13 | |
Aurintricarboxylic Acid is known to inhibit the activity of nucleases. Given that TXNDC10 is involved in the oxidative protein folding by acting in conjunction with ERp57, inhibiting nucleases can disrupt the redox state of the ER, thereby indirectly inhibiting the protein-folding function of TXNDC10. | ||||||
Ebselen | 60940-34-3 | sc-200740B sc-200740 sc-200740A | 1 mg 25 mg 100 mg | $32.00 $133.00 $449.00 | 5 | |
Ebselen is a seleno-organic compound that acts as a mimic of glutathione peroxidase and can also irreversibly inhibit thioredoxin reductase. By disrupting the thioredoxin system, ebselen can indirectly inhibit the reduction-oxidation (redox) regulation function of TXNDC10. | ||||||
PX 12 | 141400-58-0 | sc-358518 sc-358518A | 10 mg 50 mg | $130.00 $495.00 | 9 | |
PX-12 is an irreversible inhibitor of thioredoxin-1, which could lead to a disturbed intracellular redox environment affecting the activity of related proteins like TXNDC10 that depend on a balanced redox state to function. | ||||||
2-Acetylphenothiazine | 6631-94-3 | sc-223384 sc-223384A | 25 g 100 g | $74.00 $222.00 | ||
ML171 is a potent inhibitor of NADPH oxidase (NOX) which is responsible for producing ROS that are involved in the oxidative protein folding process in the ER, a process TXNDC10 is part of. Inhibition of NOX by ML171 can thus interfere with the proper functioning of TXNDC10. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $150.00 $210.00 $1899.00 | 39 | |
Auranofin is an inhibitor of thioredoxin reductase, an enzyme involved in maintaining the redox environment that TXNDC10 requires for its protein-folding function. Thus, auranofin can indirectly inhibit the function of TXNDC10. | ||||||
Salubrinal | 405060-95-9 | sc-202332 sc-202332A | 1 mg 5 mg | $33.00 $102.00 | 87 | |
Salubrinal is a selective inhibitor of eIF2α phosphatase, leading to the accumulation of phosphorylated eIF2α which is involved in the unfolded protein response. This can indirectly inhibit TXNDC10 by impairing its ability to act in response to misfolded proteins. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation, an essential process for many proteins in the ER. Inhibition of this process can lead to ER stress and dysfunctional protein folding, thus indirectly inhibiting the function of TXNDC10 in protein folding. | ||||||
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 transport, which can lead to protein misfolding and ER stress. This can indirectly inhibit the function of TXNDC10 by overwhelming its protein-folding capacity. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin is a SERCA pump inhibitor that leads to depletion of ER calcium stores, which are crucial for the function of chaperone proteins. With reduced calcium levels, the chaperone activity of TXNDC10 can be indirectly inhibited. | ||||||