EG627009 Inhibitors
Pramel15, a gene encoding a protein with predicted ubiquitin ligase-substrate adaptor activity, plays a crucial role in cellular processes by virtue of its involvement in the Cul2-RING ubiquitin ligase complex. This complex is pivotal for the regulation of protein degradation and turnover, particularly in the cytoplasm. The predicted function of Pramel15 as a substrate adaptor within this complex underscores its significance in ubiquitin-mediated degradation pathways. The gene exhibits orthologous relationships with several human genes, including PRAMEF1, PRAMEF10, and PRAMEF11, suggesting a broader functional context within the cell.
In the realm of inhibition, a diverse array of chemical compounds has been considered to modulate Pramel15 activity. Direct inhibitors disrupt ubiquitin ligase activity or interfere with the components of the Cul2-RING ubiquitin ligase complex, leading to altered stability and activity of Pramel15 in the cytoplasm. These mechanisms involve targeting specific protein-protein interactions, such as disrupting the VHL-Pramel15 interaction or inhibiting NEDD8-activating enzyme to prevent Cul2 neddylation. Indirect inhibitors, on the other hand, influence Pramel15 through various signaling pathways and cellular processes. These include modulating metabolic pathways, such as glycolysis, and affecting key cellular regulators like PI3K, AMPK, and NF-κB. By impacting these pathways, these compounds indirectly modify the dynamics of the Cul2-RING ubiquitin ligase complex, ultimately influencing Pramel15 stability and cytoplasmic activity. Understanding the functional intricacies of Pramel15 and the diverse mechanisms by which it can be modulated provides valuable insights into the regulatory networks governing cellular processes. The intricate interplay of various chemical compounds with Pramel15 highlights the complexity of its regulation and its potential as a key player in cellular homeostasis. Further exploration of these mechanisms could unravel novel aspects of cellular regulation and contribute to a deeper understanding of the molecular pathways involving Pramel15.
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Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
MLN 4924 | 905579-51-3 | sc-484814 | 1 mg | $286.00 | 1 | |
Inhibits NEDD8-activating enzyme, suppressing Cul2 neddylation and subsequent Pramel15 ubiquitination. Disrupts the Cul2-RING ubiquitin ligase complex, leading to increased Pramel15 stability and cytoplasmic activity. | ||||||
Thalidomide | 50-35-1 | sc-201445 sc-201445A | 100 mg 500 mg | $111.00 $357.00 | 8 | |
Modulates Cereblon, an E3 ubiquitin ligase substrate adaptor. Indirectly affects Pramel15 by altering Cul2-RING ubiquitin ligase complex dynamics. Consequently, Pramel15 ubiquitination and cytoplasmic activity are influenced. | ||||||
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 | $152.00 $479.00 $632.00 $1223.00 $2132.00 | 33 | |
Inhibits HDACs, leading to increased acetylation of proteins involved in the Cul2-RING ubiquitin ligase complex. Indirectly impacts Pramel15 stability and activity in the cytoplasm. | ||||||
3-(3-Pyridinyl)-1-(4-pyridinyl)-2-propene-1-one-d4 | 13309-08-5 | sc-216352 | 1 mg | $360.00 | ||
Inhibits PFKFB3, affecting glycolysis. Metabolic alteration indirectly influences Pramel15 by modifying the Cul2-RING ubiquitin ligase complex components' acetylation status, impacting Pramel15 stability and activity in the cytoplasm. | ||||||
LCL-161 | 1005342-46-0 | sc-507541 | 10 mg | $360.00 | ||
Inhibits IAPs, disrupting ubiquitin-mediated degradation pathways. Indirectly impacts Pramel15 by altering the Cul2-RING ubiquitin ligase complex dynamics, leading to enhanced Pramel15 stability and cytoplasmic activity. | ||||||
Ruxolitinib | 941678-49-5 | sc-364729 sc-364729A sc-364729A-CW | 5 mg 25 mg 25 mg | $251.00 $500.00 $547.00 | 16 | |
Inhibits JAK2, affecting the JAK-STAT pathway. Indirect influence on Pramel15 involves downstream signaling modifications, ultimately impacting the Cul2-RING ubiquitin ligase complex and Pramel15 cytoplasmic regulation. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $123.00 $400.00 | 148 | |
Inhibits PI3K, influencing the PI3K-AKT pathway. Indirect modulation impacts Pramel15 by altering Cul2-RING ubiquitin ligase complex dynamics, leading to modified Pramel15 stability and cytoplasmic activity. | ||||||
AICAR | 2627-69-2 | sc-200659 sc-200659A sc-200659B | 50 mg 250 mg 1 g | $65.00 $280.00 $400.00 | 48 | |
Activates AMPK, influencing energy metabolism. Indirectly affects Pramel15 by altering the Cul2-RING ubiquitin ligase complex dynamics through AMPK-mediated phosphorylation, leading to modified Pramel15 stability and cytoplasmic activity. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
Inhibits HSP90, impacting chaperone-mediated protein folding. Indirectly influences Pramel15 by disrupting the folding and assembly of Cul2-RING ubiquitin ligase complex components, leading to altered Pramel15 stability and cytoplasmic activity. | ||||||
BAY 11-7082 | 19542-67-7 | sc-200615B sc-200615 sc-200615A | 5 mg 10 mg 50 mg | $62.00 $85.00 $356.00 | 155 | |
Inhibits NF-κB, affecting inflammation. Indirect modulation influences Pramel15 through altered Cul2-RING ubiquitin ligase complex dynamics, leading to modified Pramel15 stability and cytoplasmic activity. | ||||||