Date published: 2026-4-24

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Dynactin 2 Inhibitors

Dynactin 2 Inhibitors, as a chemical class, broadly encompasses compounds that indirectly affect the function of Dynactin 2, a protein subunit integral to the dynactin complex, by targeting the microtubule network and associated motor proteins. This class is not defined by a specific molecular structure or target but rather by the functional impact these compounds have on cellular processes involving Dynactin 2. Primarily, these inhibitors work by modulating the dynamics of microtubules, which are critical components of the cellular cytoskeleton. Microtubules, composed of tubulin subunits, are essential for various cellular functions, including intracellular transport, where Dynactin 2 plays a role. Inhibitors like Paclitaxel and Epothilone B, for instance, stabilize microtubules by binding to β-tubulin and promoting polymerization, while others like Colchicine and Vinblastine disrupt microtubule assembly by binding to tubulin and inhibiting its polymerization Dynactin 2 Inhibitors class also includes compounds that affect other elements of the cytoskeletal network and motor proteins, highlighting the intricate interplay within the cell. For example, Cytochalasin D disrupts the organization of actin filaments, another key component of the cytoskeleton, which can indirectly influence Dynactin 2 functions. Similarly, Kinesin Inhibitor IX targets kinesin motor proteins, affecting their role in vesicle and organelle transport and, consequently, the overall transport mechanisms within the cell, including those involving Dynactin 2. These inhibitors, by modulating the functions of microtubules and related proteins, underscore the complexity of targeting a specific subunit within a larger protein complex. The varied mechanisms of these compounds reflect the multifaceted nature of cellular transport and organization, where the role of Dynactin 2 is integral yet influenced by a broader network of structural and functional proteins. The chemical diversity within this class, from microtubule-stabilizing agents to actin filament disruptors, reveals the intricate balance of forces and interactions that govern cellular dynamics and the potential of chemical compounds to modulate these processes at a fundamental level.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Epothilone B, Synthetic

152044-54-7sc-203944
2 mg
$176.00
(0)

Epothilone B stabilizes microtubules in a similar manner to Paclitaxel, potentially affecting Dynactin 2 by altering microtubule dynamics.

Docetaxel

114977-28-5sc-201436
sc-201436A
sc-201436B
5 mg
25 mg
250 mg
$87.00
$332.00
$1093.00
16
(1)

Docetaxel is a semi-synthetic analogue of Paclitaxel and can indirectly affect Dynactin 2 by stabilizing microtubules and inhibiting their disassembly.

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 inhibits microtubule assembly, which can indirectly inhibit Dynactin 2 by affecting the microtubule network.

Combrestatin A4

117048-59-6sc-204697
sc-204697A
1 mg
5 mg
$46.00
$81.00
(0)

Combretastatin A4 binds to tubulin and disrupts microtubule formation, potentially affecting Dynactin 2 by altering the microtubule network it relies on for function.

Maytansine

35846-53-8sc-507510
100 mg
$1000.00
(0)

Maytansine is a potent microtubule-targeting agent that inhibits tubulin polymerization, which can indirectly inhibit Dynactin 2.

Estramustine

2998-57-4sc-353281
sc-353281A
100 mg
1 g
$265.00
$743.00
(0)

Estramustine binds to tubulin and inhibits microtubule polymerization, potentially impacting Dynactin 2 function by affecting the microtubule network.

Podophyllotoxin

518-28-5sc-204853
100 mg
$84.00
1
(1)

Podophyllotoxin inhibits tubulin polymerization, which can indirectly affect Dynactin 2 by disrupting the microtubule network it relies on.

Griseofulvin

126-07-8sc-202171A
sc-202171
sc-202171B
5 mg
25 mg
100 mg
$85.00
$220.00
$598.00
4
(2)

Griseofulvin disrupts microtubule dynamics by binding to tubulin, potentially affecting Dynactin 2 by altering its functional environment.