Date published: 2025-12-24

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Septin 14 Inhibitors

Septin 14 Inhibitors are a specialized class of chemical compounds designed to specifically target and inhibit the activity of Septin 14, a member of the septin family of GTP-binding proteins. Septin 14 plays a significant role in cellular processes such as cytokinesis, cell division, and the maintenance of cellular architecture by forming filamentous structures that interact with the cytoskeleton. These inhibitors function by binding to critical regions of the Septin 14 protein, particularly the GTP-binding domain or the interfaces that mediate septin-septin interactions, which are essential for the polymerization and organization of septin filaments. By blocking these interactions, Septin 14 Inhibitors can prevent the formation of the filamentous structures that are crucial for the protein's function, leading to alterations in the organization and stability of the cytoskeleton and potentially disrupting key cellular processes.

The effectiveness of Septin 14 Inhibitors is heavily dependent on their chemical structure and properties. These inhibitors are often designed to closely resemble the natural ligands of Septin 14, such as GTP or GDP, allowing them to compete effectively for binding to the GTP-binding domain. Additionally, these compounds may feature structural elements that enable them to disrupt protein-protein interactions within the septin complex, preventing the stable assembly of septin filaments. The molecular design typically includes specific functional groups that enhance the binding affinity to Septin 14, such as groups capable of forming hydrogen bonds or engaging in hydrophobic interactions with key amino acid residues in the protein. The solubility, stability, and overall bioavailability of these inhibitors are optimized to ensure they can efficiently reach and act on Septin 14 within the cellular environment. Furthermore, the kinetics of binding, including how quickly the inhibitor associates with and dissociates from Septin 14, are critical factors that influence the potency and duration of inhibition. By studying the interaction between Septin 14 Inhibitors and their target protein, researchers can gain a deeper understanding of the role of Septin 14 in cellular organization and the broader implications of disrupting its function in various cellular processes.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
$260.00
$799.00
36
(2)

Latrunculin A binds to actin and prevents its polymerization. Septin 14 is known to interact with actin filaments during cell division, so by destabilizing actin filaments, Latrunculin A can inhibit the proper function of Septin 14 in the process of cytokinesis.

Swinholide A, Theonella swinhoei

95927-67-6sc-205914
10 µg
$135.00
(0)

Swinholide A sequesters actin dimers and prevents actin polymerization. Because Septin 14 is associated with actin dynamics during cell division, Swinholide A can inhibit the function of Septin 14 by disturbing the actin cytoskeleton and thus interfering with Septin 14's role in cytokinesis.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$145.00
$442.00
64
(4)

Cytochalasin D binds to the barbed ends of actin filaments, blocking polymerization and elongation. This disruption of actin dynamics can inhibit Septin 14's ability to function properly during cell division, particularly during the formation of the cleavage furrow where septins are key.

Nocodazole

31430-18-9sc-3518B
sc-3518
sc-3518C
sc-3518A
5 mg
10 mg
25 mg
50 mg
$58.00
$83.00
$140.00
$242.00
38
(2)

Nocodazole is a microtubule-depolymerizing agent. It inhibits microtubule polymerization and can lead to mitotic arrest. As Septin 14 interacts with microtubules during cell division, Nocodazole's action on microtubules can inhibit the necessary functions of Septin 14 during mitotic spindle formation and cytokinesis.

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
$98.00
$315.00
$2244.00
$4396.00
$17850.00
$34068.00
3
(2)

Colchicine binds to tubulin, inhibiting its polymerization into microtubules. Since Septin 14 is involved in mitotic spindle stability, the inhibition of microtubule polymerization by Colchicine would impede Septin 14's function in maintaining the integrity of the spindle apparatus.

Vinblastine

865-21-4sc-491749
sc-491749A
sc-491749B
sc-491749C
sc-491749D
10 mg
50 mg
100 mg
500 mg
1 g
$100.00
$230.00
$450.00
$1715.00
$2900.00
4
(0)

Vinblastine binds to tubulin and inhibits microtubule formation. As Septin 14 is involved in microtubule-dependent processes during cell division, Vinblastine's inhibition of microtubule assembly can disrupt Septin 14's role in mitosis and cytokinesis.

Griseofulvin

126-07-8sc-202171A
sc-202171
sc-202171B
5 mg
25 mg
100 mg
$83.00
$216.00
$586.00
4
(2)

Griseofulvin disrupts microtubule function by binding to tubulin and interfering with its polymerization. This action can inhibit Septin 14 by destabilizing the microtubules that are necessary for Septin 14's proper function during cell division.

Epothilone B, Synthetic

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

Epothilone B binds to tubulin and leads to microtubule stabilization, much like Paclitaxel. This stabilization can inhibit Septin 14 by disrupting the normal microtubule dynamics that are essential for its function in the process of cell division and cytokinesis.