Inhibitors of FAM158A function by interfering with various aspects of cellular homeostasis, primarily targeting the endoplasmic reticulum (ER) where this protein exerts its effects. Compounds that inhibit the mechanistic target of rapamycin (mTOR) pathway induce a cellular state that can lead to the accumulation of misfolded proteins within the ER, thereby creating a stressful environment that can indirectly inhibit the function of FAM158A. The ER is the site of protein folding and maturation, and when this process is disrupted, either through the inhibition of mTOR or by compounds that directly interfere with N-linked glycosylation, the ability of FAM158A to carry out its role within the ER membrane protein complex is compromised. Moreover, some compounds disrupt protein transport by inhibiting factors essential for the maintenance of the Golgi apparatus structure, which is closely linked to ER function, thus affecting the operational capacity of FAM158A within the ER-Golgi transport pathway.
Additionally, ER stress is a common theme in the inhibition of FAM158A, with several inhibitors targeting different aspects of ER homeostasis. Chemical chaperones, for instance, are involved in aiding protein folding within the ER, and their inhibition can exacerbate the stress on the ER, potentially overloading its capacity to deal with misfolded proteins and causing a detrimental effect on FAM158A function. Furthermore, inhibitors that modulate calcium release from the ER can affect the protein folding environment, as calcium ions play a crucial role in the function of many ER-resident enzymes and chaperones. By disturbing the calcium balance, these compounds can indirectly influence the ability of FAM158A to function properly. In addition, agents that induce the unfolded protein response (UPR) can lead to a reduction in the overall protein synthesis rates, which might help to alleviate ER stress but could also limit the synthesis and functionality of FAM158A.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $62.00 $155.00 $320.00 | 233 | |
This compound inhibits mTOR, a kinase that regulates cell growth and proliferation, by directly binding to it and inhibiting its activity. FAM158A is part of the ER membrane protein complex which is involved in protein folding and maturation. Inhibition of mTOR can lead to a buildup of misfolded proteins, indirectly inhibiting the function of FAM158A by overstressing ER functions. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
An inhibitor of N-linked glycosylation which disrupts protein folding in the ER. FAM158A, being part of the ER membrane protein complex, could see its function indirectly inhibited due to the accumulation of misfolded glycoproteins and ER stress. | ||||||
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 | |
This compound disrupts protein transport by inhibiting the ADP-ribosylation factor, leading to the disassembly of the Golgi apparatus. Since FAM158A is involved in ER to Golgi transport, its functional activity can be indirectly inhibited as a result. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
A SERCA pump inhibitor that leads to increased cytosolic calcium levels and induces ER stress. As FAM158A is part of the ER protein complex, its function could be indirectly inhibited due to heightened ER stress and the unfolded protein response. | ||||||
Cyclopiazonic Acid | 18172-33-3 | sc-201510 sc-201510A | 10 mg 50 mg | $173.00 $612.00 | 3 | |
An inhibitor of the SERCA pump that increases cytosolic calcium and induces ER stress, which could indirectly inhibit FAM158A function by disrupting ER homeostasis. | ||||||
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 | |
A proteasome inhibitor that leads to the accumulation of misfolded proteins, causing ER stress and potentially inhibiting the function of FAM158A as part of the ER protein complex responding to misfolded proteins. | ||||||
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 | |
An inhibitor of ER-associated degradation (ERAD) that can lead to ER stress and potentially inhibit FAM158A activity by disrupting its role in the ER protein complex. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
By inhibiting autophagy and lysosomal degradation, this compound can cause an accumulation of misfolded proteins in the ER, which could indirectly inhibit FAM158A's function within the ER protein complex. | ||||||
Sodium phenylbutyrate | 1716-12-7 | sc-200652 sc-200652A sc-200652B sc-200652C sc-200652D | 1 g 10 g 100 g 1 kg 10 kg | $75.00 $163.00 $622.00 $4906.00 $32140.00 | 43 | |
A chemical chaperone that reduces ER stress by assisting in protein folding, potentially leading to an indirect inhibition of FAM158A function by altering ER homeostasis and the need for the ER protein complex. | ||||||
DBeQ | 177355-84-9 | sc-499943 | 10 mg | $330.00 | 1 | |
An ATPase inhibitor of the p97 complex involved in ERAD, potentially leading to ER stress and indirectly inhibiting FAM158A's role in the ER protein complex. |