UBL4A Inhibitors
Inhibitors that affect UBL4A function operate through mechanisms that disturb various cellular processes essential for maintaining protein homeostasis, which UBL4A is intricately involved with. Compounds that inhibit the action of molecular chaperones like HSP90 result in the destabilization of their client proteins, which indirectly impacts the functional activity of UBL4A by overloading the protein quality control system with an excess of misfolded proteins. Similarly, proteasome inhibitors lead to an accumulation of polyubiquitinated proteins awaiting degradation, indirectly challenging the capacity of UBL4A-related pathways to manage these proteins effectively. Inhibitors that interfere with normal cell division mechanics can reduce the necessity for UBL4A's role in mitosis, as the cell cycle is arrested and the demand for protein folding within this context is diminished.
Moreover, compounds that disrupt protein biosynthesis at various stages-whether by halting translational elongation or causing premature chain termination-can lower the functional requirement for UBL4A's protein-folding assistance due to a reduction in nascent protein production. Other inhibitors that induce ER stress or impede ER-associated degradation cause an excess of misfolded proteins within the ER, further burdening the protein quality control system and indirectly reducing UBL4A activity. Disruption of cytoskeletal components and intracellular transport mechanisms also indirectly affects UBL4A function by hindering the proper localization and distribution of protein complexes that UBL4A is associated with, emphasizing the interconnectivity of UBL4A's role within the broader landscape of cellular homeostasis.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
MLN8237 | 1028486-01-2 | sc-394162 | 5 mg | $220.00 | ||
This Aurora kinase A inhibitor leads to disruption of the mitotic spindle assembly, which is crucial for cell division. UBL4A, being part of the protein quality control system, is indirectly inhibited as the demand for proper folding and function of proteins involved in mitosis is decreased due to cell cycle arrest. | ||||||
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 | |
HSP90 inhibitor that destabilizes client proteins by preventing their proper folding. As UBL4A is implicated in protein folding processes, the inhibition of HSP90 can indirectly lead to decreased functional activity of UBL4A due to the accumulation of misfolded proteins overwhelming the protein quality control system. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
An N-linked glycosylation inhibitor that disrupts protein folding within the ER, leading to ER stress and activation of the unfolded protein response. UBL4A is involved in protein folding and ER-associated degradation; thus, tunicamycin indirectly inhibits UBL4A by increasing its substrate load beyond capacity. | ||||||
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 polyubiquitinated proteins, which can overload the protein degradation machinery. Since UBL4A is part of the protein quality control system, its function is indirectly inhibited by the backlog of proteins requiring degradation. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
A proteasome inhibitor that similarly causes the accumulation of proteins targeted for degradation, indirectly inhibiting UBL4A by overwhelming the protein quality control system, of which UBL4A is a component. | ||||||
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $40.00 $82.00 $256.00 | 127 | |
An inhibitor of eukaryotic protein biosynthesis that prevents the translational elongation step in protein synthesis. By halting protein synthesis, the functional role of UBL4A in protein folding and stabilization is indirectly minimized as there are fewer nascent proteins to assist. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
A SERCA pump inhibitor leading to increased cytosolic calcium levels and ER stress, which in turn can overload the protein folding capacity of the ER. UBL4A, involved in ER-associated protein quality control, is indirectly inhibited due to the heightened stress response. | ||||||
Puromycin | 53-79-2 | sc-205821 sc-205821A | 10 mg 25 mg | $163.00 $316.00 | 436 | |
Causes premature chain termination during protein synthesis. As UBL4A assists in protein folding, its activity is indirectly inhibited when there is a reduction in the total number of newly synthesized proteins needing such assistance. | ||||||
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 that can cause an accumulation of misfolded proteins in the ER. UBL4A's role in managing ER stress is indirectly inhibited as protein quality control mechanisms become overwhelmed. | ||||||
Salubrinal | 405060-95-9 | sc-202332 sc-202332A | 1 mg 5 mg | $33.00 $102.00 | 87 | |
A selective inhibitor of eIF2α dephosphorylation that leads to attenuation of global protein synthesis. This indirectly inhibits UBL4A by reducing the demand for its protein folding assistance as fewer proteins are synthesized. | ||||||