ACTL8 inhibitors comprise a diverse set of chemical compounds that exert their inhibitory effects through various mechanisms centered on the disruption of actin dynamics, with which ACTL8 is intricately involved. Taxol, by stabilizing microtubules, indirectly hinders ACTL8 function by altering the cellular balance between microtubules and actin filaments, critical for proper cell division and cytoskeletal integrity. Similarly, Cytochalasin D and Latrunculin A impede actin polymerization, thereby directly undermining the structural framework that ACTL8 operates within. Swinholide A and Bedaquiline, both actin-disrupting agents, function by severing actin filaments and inhibiting polymerization, respectively, leading to a reduction in ACTL8 activity, which is reliant on the formation and maintenance of actin structures. Jasplakinolide and Phalloidin, although actin stabilizers, can paradoxically result in the functional inhibition of ACTL8 by preventing the normal turnover of actin filaments essential for ACTL8's role.
Continuing with the theme of cytoskeletal interference, Y-27632 and Blebbistatin target proteins upstream of actin filament formation, such as Rho-associated protein kinase and myosin II, respectively. The diminished activity of these proteins leads to a reduction in actin filament stability and tension, consequently decreasing ACTL8's ability to bind and stabilize these structures. ML-7's inhibition of myosin light chain kinase further contributes to the reduction of actin-myosin interactions, essential for the actin filament dynamics involved in ACTL8's function. Withaferin A disrupts actin organization by binding to annexin II, thereby indirectly inhibiting ACTL8's activity. Lastly, NSC 23766 targets formins, inhibiting the nucleation and elongation of actin filaments, which are necessary for the formation of the complex actin structures where ACTL8 is active, culminating in a comprehensive suppression of ACTL8's functional capacity.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $41.00 $74.00 $221.00 $247.00 $738.00 $1220.00 | 39 | |
Taxol stabilizes microtubules and as a result, inhibits their disassembly, which is crucial for cell division. Since ACTL8 is involved in the organization of actin filaments, paclitaxel's stabilization of microtubules can lead to a diminished function of ACTL8 by disrupting the dynamic equilibrium between the actin and microtubule networks. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D binds to the barbed ends of actin filaments, preventing polymerization and elongation. This directly leads to a decreased functional activity of ACTL8 by disrupting the formation of the actin cytoskeleton where ACTL8 operates. | ||||||
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 prevents their polymerization. This destabilizes the actin cytoskeleton and thus directly diminishes the activity of ACTL8 by impeding the formation of actin fibers that ACTL8 would normally stabilize or bind to. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide stabilizes actin filaments and prevents their depolymerization. The hyperstabilization of actin filaments can paradoxically inhibit the functional activity of ACTL8 by preventing the normal cycling of actin monomers and filaments, which is necessary for ACTL8's role in actin dynamics. | ||||||
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $234.00 | 33 | |
Phalloidin binds tightly to F-actin, stabilizing it against disassembly. This hyperstabilization can indirectly diminish ACTL8 activity by fixing actin filaments in a rigid state, not conducive to the dynamic remodeling required for ACTL8's functional roles. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
Y-27632 is a Rho-associated protein kinase (ROCK) inhibitor. Since ROCK is involved in actin filament stabilization and stress fiber formation, inhibition by Y-27632 can lead to reduced actin filament stability, thereby diminishing ACTL8's functional capacity to bind to and stabilize these structures. | ||||||
(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, a motor protein that interacts with actin filaments for muscle contraction and cell motility. Inhibition of myosin II activity can lead to a disruption of actin-myosin interaction, which can diminish ACTL8 activity by altering the actin structures that ACTL8 would typically associate with. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which phosphorylates myosin light chains to promote actin-myosin interaction. By inhibiting MLCK, ML-7 can diminish ACTL8 activity by reducing the formation and tension of actin-myosin fibers, where ACTL8 is implicated in stabilizing actin filaments. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $130.00 $583.00 $4172.00 $20506.00 | 20 | |
Withaferin A binds to annexin II and is known to disrupt the actin cytoskeleton. By altering the actin dynamics and organization, Withaferin A indirectly diminishes the activity of ACTL8, which relies on a properly organized actin network for its function. | ||||||