WIRE Inhibitors
Chemical inhibitors of WIRE act through a variety of mechanisms to disrupt the protein's function, which is closely associated with the dynamics of the actin cytoskeleton. Cytochalasin D, for example, directly impedes the polymerization of actin filaments, preventing the formation of structures that WIRE is known to stabilize and interact with. This leads to a functional inhibition of WIRE as it can no longer bind to its primary target, actin, thus impairing the cellular processes in which it is involved. Similarly, Latrunculin A sequesters actin monomers, effectively depriving WIRE of the substrate it needs to function, while Swinholide A severs existing actin filaments, further destabilizing the cytoskeleton and disrupting WIRE's role in actin filament stabilization.
The actin cytoskeleton's architecture is also targeted by compounds such as Phalloidin, which hyper-stabilize actin filaments. This excessive stabilization creates an abnormal state of the actin cytoskeleton, which can prevent WIRE from performing its normal regulatory functions. Y-27632 and ML-7 disrupt downstream signaling pathways and actin-myosin interactions, respectively. By inhibiting Rho-associated protein kinase with Y-27632, the organization of actin filaments that WIRE interacts with is altered, leading to an inhibition of WIRE's functional role. ML-7's inhibition of myosin light chain kinase similarly affects actin-myosin interactions, which are essential for a range of cellular processes. Furthermore, Blebbistatin's inhibition of myosin II ATPase activity can impede actin-myosin-driven cellular functions, leading to an indirect inhibition of WIRE. Lastly, inhibitors like SMIFH2 and CK-666 act by disrupting actin nucleation processes, with SMIFH2 targeting formin-mediated actin formation and CK-666 inhibiting the Arp2/3 complex responsible for actin branching, all of which can inhibit the formation of actin networks and thus WIRE's ability to stabilize and interact with these structures.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D disrupts actin polymerization, and since WIRE is known to bind to actin, inhibiting actin filament formation can lead to functional inhibition of WIRE by preventing it from interacting with its primary binding partner, thus impairing the cellular processes WIRE is involved in. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers and sequesters them, preventing their polymerization. As WIRE stabilizes actin filaments, Latrunculin A's sequestration of actin monomers can inhibit WIRE function by disrupting the actin cytoskeleton structure it relies on. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A severs actin filaments and prevents their reannealing. The resulting depolymerization of actin filaments can inhibit WIRE by destabilizing the actin structures that WIRE is known to stabilize, thus impairing its function in actin-mediated cellular processes. | ||||||
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $234.00 | 33 | |
Phalloidin binds to and stabilizes actin filaments. This stabilization inhibits WIRE by effectively "freezing" the actin filaments in a state that prevents them from participating in dynamic cellular functions where WIRE might normally play a role, such as cell migration or signaling. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 inhibits ROCK (Rho-associated protein kinase), which is involved in actin cytoskeleton organization. By inhibiting ROCK, Y-27632 can lead to a disruption of actin filament organization that WIRE is a part of, thus inhibiting WIRE's ability to interact with properly organized actin structures. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7 inhibits myosin light chain kinase (MLCK), which is involved in actin-myosin contraction. By inhibiting MLCK, there is a decrease in actin-myosin interactions that are crucial for many cellular processes. This can inhibit WIRE indirectly by reducing the functional interactions of actin where WIRE is active. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $72.00 $265.00 $495.00 $968.00 | ||
Blebbistatin inhibits myosin II ATPase activity, which is essential for muscle contraction and cell motility involving actin dynamics. Inhibiting this activity can lead to functional inhibition of WIRE by impairing actin-myosin-driven processes that WIRE is associated with. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 inhibits formin-mediated actin nucleation and elongation, key processes in actin filament formation. By inhibiting formins, SMIFH2 can functionally inhibit WIRE by disrupting the formation of actin structures that WIRE needs for its stabilization function within the cell. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
CK-666 is an inhibitor of the Arp2/3 complex, which is involved in the nucleation of new actin filaments. Inhibiting Arp2/3-mediated actin branching can inhibit WIRE function by preventing the formation of actin networks that WIRE would typically stabilize and interact with. | ||||||
CCG-1423 | 285986-88-1 | sc-205241 sc-205241A | 1 mg 5 mg | $30.00 $90.00 | 8 | |
CCG-1423 inhibits RhoA signaling, which is important for actin cytoskeleton dynamics. By inhibiting RhoA, CCG-1423 can functionally inhibit WIRE by disrupting the signaling pathways that lead to actin cytoskeleton reorganization, a process in which WIRE is known to play a significant role. | ||||||