Date published: 2026-4-10

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tropomodulin 2 Inhibitors

Chemical inhibitors of tropomodulin 2 can disrupt its function through various mechanisms involving the alteration of cytoskeletal dynamics. Colchicine, which binds to tubulin, can disrupt the microtubule dynamics that tropomodulin 2 relies on for the stabilization of actin filaments. Similarly, Vinblastine's interference with microtubule assembly results in a disturbance of the cytoskeletal balance, indirectly affecting the actin capping role of tropomodulin 2. In contrast, Cytochalasin D and Latrunculin A directly target actin filaments, the primary substrate for tropomodulin 2's function. Cytochalasin D binds to the barbed ends of actin filaments, preventing their elongation, while Latrunculin A sequesters actin monomers, inhibiting their polymerization and thus, the formation of filaments for tropomodulin 2 to cap. Furthermore, Misakinolide A stabilizes actin filaments, which can render the capping action of tropomodulin 2 redundant or disrupted, as the dynamics of actin polymerization are altered. Swinholide A and Chondramide act by severing actin filaments and disrupting their polymerization, respectively, which leads to a reduced number of filaments available for tropomodulin 2 to cap and stabilize. Pertussis Toxin affects signaling pathways and kinase activities that are upstream of the actin assembly process. By altering the cellular signaling context, these inhibitors can indirectly reduce the functional necessity or the ability of tropomodulin 2 to maintain actin filament integrity.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Colchicine

64-86-8sc-203005
sc-203005A
sc-203005B
sc-203005C
sc-203005D
sc-203005E
1 g
5 g
50 g
100 g
500 g
1 kg
$100.00
$321.00
$2289.00
$4484.00
$18207.00
$34749.00
3
(2)

Colchicine binds to tubulin, disrupting microtubule dynamics, which tropomodulin 2 stabilizes by capping the pointed ends of actin filaments. Disruption of microtubules can lead to the destabilization of the entire cytoskeletal network, thereby functionally inhibiting the stabilizing action of tropomodulin 2 on actin filaments.

Vinblastine

865-21-4sc-491749
sc-491749A
sc-491749B
sc-491749C
sc-491749D
10 mg
50 mg
100 mg
500 mg
1 g
$102.00
$235.00
$459.00
$1749.00
$2958.00
4
(0)

Vinblastine interferes with microtubule assembly. Since tropomodulin 2's action is closely related to the cytoskeletal integrity, the disturbance in microtubule dynamics caused by vinblastine can indirectly inhibit the function of tropomodulin 2 by altering the cytoskeletal architecture on which it acts.

Cytochalasin D

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

Cytochalasin D binds to the barbed ends of actin filaments, preventing polymerization and elongation. This action can inhibit the role of tropomodulin 2 in maintaining actin filament dynamics by capping the pointed ends, as the overall polymerization state of actin is compromised.

Latrunculin A, Latrunculia magnifica

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

Latrunculin A binds to actin monomers and prevents their polymerization, which can inhibit the function of tropomodulin 2 by removing the substrate (actin filaments) it normally caps and stabilizes.

Swinholide A, Theonella swinhoei

95927-67-6sc-205914
10 µg
$135.00
(0)

Swinholide A severs actin filaments and binds to actin dimers, which can inhibit tropomodulin 2's function by disrupting existing actin filaments and preventing the formation of new ones that tropomodulin 2 would normally stabilize.

Pertussis Toxin (islet-activating protein)

70323-44-3sc-200837
50 µg
$451.00
3
(1)

Pertussis Toxin inhibits G-protein coupled receptor signaling, which can lead to changes in intracellular actin dynamics and functionally inhibit tropomodulin 2 by altering the cellular context in which it operates.

Y-27632, free base

146986-50-7sc-3536
sc-3536A
5 mg
50 mg
$186.00
$707.00
88
(1)

Y-27632 inhibits the Rho-associated kinase (ROCK), which can lead to decreased phosphorylation of downstream targets that affect actin filament assembly and stability. This may inhibit the function of tropomodulin 2 since it relies on the proper formation and dynamics of actin filaments to exert its stabilizing effect.