Ruvbl2 Inhibitors
Chemical inhibitors of Ruvbl2 interfere with its function in a variety of ways, each chemical exhibiting a unique mode of action. Suramin competes with ATP for binding sites on Ruvbl2, which is fundamental for its ATPase activity. This competition impairs Ruvbl2's ability to participate in energy-dependent processes such as chromatin remodeling and transcriptional regulation. Similarly, Griseofulvin disrupts microtubule dynamics by binding and inhibiting their polymerization, which is crucial for the protein complexes that Ruvbl2 is a part of, especially those associated with cell division and mitosis. Additionally, both Epothilone B and Ixabepilone stabilize microtubules, but this stabilization leads to an indirect inhibition of Ruvbl2 by affecting the normal function of protein complexes that associate with microtubules. Cilengitide, on the other hand, impacts Ruvbl2 by disrupting integrin-mediated cell adhesion, a process in which Ruvbl2 is thought to play a signaling role. Moreover, Tivantinib, primarily a kinase inhibitor, potentially impacts multiple signaling pathways involving Ruvbl2, although it does not target Ruvbl2 directly. Temozolomide's action involves modifying the DNA structure, which can influence Ruvbl2's involvement in DNA repair mechanisms.
Furthermore, Auranofin inhibits thioredoxin reductase, leading to oxidative stress that may affect Ruvbl2 by damaging the proteins or nucleic acids it interacts with. Disulfiram contributes to the inhibition of Ruvbl2 through its action on the proteasome, leading to an accumulation of proteins that may overwhelm the cellular quality control systems involving Ruvbl2. MK-2206 targets AKT, a kinase that is part of several pathways including those associated with Ruvbl2's functions, hence affecting Ruvbl2 indirectly. Bortezomib, another proteasome inhibitor, causes protein accumulation which could disrupt the protein homeostasis systems that Ruvbl2 is part of. Lastly, Geldanamycin binds to Hsp90, inhibiting its activity and potentially destabilizing the multi-protein complexes that rely on Hsp90 and include Ruvbl2, affecting its functional participation within these complexes.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Suramin sodium | 129-46-4 | sc-507209 sc-507209F sc-507209A sc-507209B sc-507209C sc-507209D sc-507209E | 50 mg 100 mg 250 mg 1 g 10 g 25 g 50 g | $152.00 $214.00 $728.00 $2601.00 $10965.00 $21838.00 $41096.00 | 5 | |
Suramin inhibits the ATPase activity of Ruvbl2 by competing with ATP binding, thereby impairing the energy-driven molecular motor functions of Ruvbl2 essential for its role in chromatin remodeling and transcriptional regulation. | ||||||
Griseofulvin | 126-07-8 | sc-202171A sc-202171 sc-202171B | 5 mg 25 mg 100 mg | $85.00 $220.00 $598.00 | 4 | |
Griseofulvin binds to microtubules and disrupts their polymerization. As Ruvbl2 is involved in the assembly of protein complexes that interact with microtubules, the disturbance of microtubule dynamics hampers Ruvbl2's function in cellular processes such as mitosis and cell division. | ||||||
Epothilone B, Synthetic | 152044-54-7 | sc-203944 | 2 mg | $176.00 | ||
Epothilone B stabilizes microtubules and as a consequence, can inhibit the Ruvbl2-associated protein complexes from carrying out their roles in chromatin remodeling and transcriptional regulation due to the perturbation of normal microtubule dynamics. | ||||||
Cilengitide | 188968-51-6 | sc-507335 | 5 mg | $215.00 | ||
Cilengitide disrupts integrin-mediated cell adhesion. Given that Ruvbl2 is implicated in cellular signaling pathways that involve integrin functions, the disruption of integrin signaling could impede Ruvbl2's role in these pathways. | ||||||
ATM/ATR Kinase Inhibitor Inhibitor | 905973-89-9 | sc-202964 | 5 mg | $106.00 | 8 | |
Tivantinib is a kinase inhibitor that, while primarily targeting MET, can disrupt various signaling pathways. Ruvbl2's associated protein complexes are involved in pathways that are regulated by kinases; thus, Tivantinib could indirectly inhibit Ruvbl2's function by disrupting these signaling pathways. | ||||||
Temozolomide | 85622-93-1 | sc-203292 sc-203292A | 25 mg 100 mg | $91.00 $255.00 | 32 | |
Temozolomide alkylates/methylates DNA, which can lead to the disruption of DNA repair processes. Ruvbl2 functions in DNA damage response; therefore, the presence of temozolomide could impede Ruvbl2's role in the assembly of protein complexes involved in DNA repair. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $153.00 $214.00 $4000.00 | 39 | |
Auranofin inhibits thioredoxin reductase, which is involved in maintaining the cellular redox environment. The inhibition of this enzyme can lead to oxidative stress, which may interfere with Ruvbl2's function by oxidatively damaging the proteins or nucleic acids that Ruvbl2 interacts with. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Disulfiram can inhibit proteasome activity, which could lead to the accumulation of misfolded or damaged proteins. This accumulation can overwhelm the protein quality control systems that Ruvbl2 is a part of, indirectly inhibiting its function. | ||||||
MK-2206 dihydrochloride | 1032350-13-2 | sc-364537 sc-364537A | 5 mg 10 mg | $182.00 $332.00 | 67 | |
MK-2206 is an allosteric inhibitor of AKT, a kinase involved in many cellular pathways, including those associated with Ruvbl2's functions. By inhibiting AKT, MK-2206 could impede the pathways that regulate Ruvbl2's role in cellular signaling and transcriptional regulation. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $135.00 $1085.00 | 115 | |
Bortezomib is a proteasome inhibitor, which can cause the build-up of proteins that are normally degraded. This accumulation can disrupt the protein homeostasis that Ruvbl2 is part of, indirectly inhibiting its function in the cell. | ||||||