Date published: 2026-5-13

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ACT Inhibitors

Chemical inhibitors of ACT can effectively disrupt its function through various mechanisms that directly target the actin cytoskeleton. Sodium Azide, for instance, undermines the cellular energy production by inhibiting cytochrome c oxidase, essential for ATP synthesis. This reduction in ATP availability is critical for actin polymerization, thereby inhibiting ACT. Similarly, Cytochalasin D binds to the barbed ends of actin filaments, halting the addition of new monomers and directly preventing ACT polymerization. Latrunculin A, on the other hand, sequesters actin monomers, which blocks the formation of actin filaments and thus inhibits ACT. Swinholide A exerts its inhibitory effect by severing actin filaments, directly reducing the amount of polymerized actin available for ACT activity. Jasplakinolide operates by stabilizing actin filaments, which leads to a depletion of the actin monomer pool necessary for filament dynamics, resulting in ACT inhibition.

Continuing with the mechanisms of inhibition, Chondramide binds to and inhibits the elongation of actin filaments, disrupting ACT dynamics. Phalloidin has a high affinity for F-actin, and its binding promotes filament stabilization while also preventing depolymerization, causing a scarcity of actin monomers required for ACT function. Tropodithietic Acid directly blocks actin polymerization, essential for ACT activity. Misakinolide A prevents the assembly of actin filaments by binding to ACT, thus directly inhibiting its function. Brefeldin A indirectly inhibits ACT by disrupting Golgi structure and subsequent vesicle transport processes that rely on actin dynamics. Mycalolide B binds to actin filaments, inducing depolymerization and reducing the polymerized actin necessary for ACT's role in maintaining cellular structure. Lastly, Sanguinarine binds to G-actin, obstructing the polymerization of actin filaments and consequently inhibiting the function of ACT, as the dynamic balance between G-actin and F-actin is critical for the protein's role in various cellular activities.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Sodium azide

26628-22-8sc-208393
sc-208393B
sc-208393C
sc-208393D
sc-208393A
25 g
250 g
1 kg
2.5 kg
100 g
$43.00
$155.00
$393.00
$862.00
$90.00
8
(2)

Inhibits ACT by interfering with the heme group of cytochrome c oxidase in the mitochondrial electron transport chain, which is essential for ATP production, leading to reduced energy availability for actin polymerization and subsequent inhibition of ACT function.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$165.00
$486.00
64
(4)

Binds to the barbed end of actin filaments, preventing the addition of new monomers, thus directly inhibiting the polymerization of ACT and leading to functional inhibition.

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$265.00
$815.00
36
(2)

Sequesters actin monomers and prevents their polymerization, directly inhibiting ACT by blocking the formation of actin filaments, a critical component of the cytoskeletal structure that ACT is involved in.

Swinholide A, Theonella swinhoei

95927-67-6sc-205914
10 µg
$135.00
(0)

Binds to ACT and severs actin filaments, thereby directly decreasing the amount of filamentous actin and inhibiting ACT activity.

Jasplakinolide

102396-24-7sc-202191
sc-202191A
50 µg
100 µg
$184.00
$305.00
59
(1)

Stabilizes actin filaments and prevents their depolymerization, which paradoxically results in functional inhibition of ACT by effectively depleting the pool of actin monomers required for filament turnover and dynamics.

Phalloidin

17466-45-4sc-202763
1 mg
$234.00
33
(1)

Binds tightly to F-actin, stabilizing it and preventing filament depolymerization, which leads to a decrease in the available actin monomers for polymerization, thereby inhibiting ACT function.

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$31.00
$53.00
$124.00
$374.00
25
(3)

Disrupts the structure of the Golgi apparatus, indirectly inhibiting ACT by affecting the vesicular transport processes that are dependent on actin dynamics, leading to functional inhibition of the protein.

Sanguinarium

2447-54-3sc-473396
10 mg
$220.00
(0)

Interferes with actin filament formation and can bind to G-actin, inhibiting the polymerization and thus the function of ACT, as the dynamic equilibrium between G-actin and F-actin is crucial for the protein's role in cellular processes.