Date published: 2025-10-10

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Septin 14 抑制因子

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.

関連項目

产品名称CAS #产品编号数量价格应用排名

Latrunculin A, Latrunculia magnifica

76343-93-6sc-202691
sc-202691B
100 µg
500 µg
¥2933.00
¥9014.00
36
(2)

拉图菌素A与肌动蛋白结合,阻止其聚合。已知在细胞分裂过程中,14号分隔蛋白与肌动蛋白丝相互作用,因此拉图菌素A通过破坏肌动蛋白丝的稳定性,抑制分隔蛋白14在细胞分裂过程中的正常功能。

Swinholide A, Theonella swinhoei

95927-67-6sc-205914
10 µg
¥1523.00
(0)

鞘氨醇内酯 A 能封存肌动蛋白二聚体,阻止肌动蛋白聚合。由于Septin 14与细胞分裂过程中的肌动蛋白动力学有关,Swinholide A可通过扰乱肌动蛋白细胞骨架来抑制Septin 14的功能,从而干扰Septin 14在细胞分裂中的作用。

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
¥1636.00
¥4987.00
64
(4)

细胞松弛素 D 可与肌动蛋白丝的倒钩末端结合,阻止其聚合和伸长。这种对肌动蛋白动态的破坏会抑制 Septin 14 在细胞分裂过程中正常发挥作用的能力,尤其是在形成裂沟的过程中,而 septins 是裂沟的关键。

Nocodazole

31430-18-9sc-3518B
sc-3518
sc-3518C
sc-3518A
5 mg
10 mg
25 mg
50 mg
¥654.00
¥936.00
¥1579.00
¥2730.00
38
(2)

Nocodazole 是一种微管解聚剂。它能抑制微管聚合,导致有丝分裂停止。由于肽蛋白 14 在细胞分裂过程中与微管相互作用,Nocodazole 对微管的作用可抑制肽蛋白 14 在有丝分裂纺锤体形成和细胞分裂过程中的必要功能。

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
¥1106.00
¥3554.00
¥25317.00
¥49596.00
¥201384.00
¥384355.00
3
(2)

秋水仙碱能与微管蛋白结合,抑制其聚合成微管。由于七叶苷 14 参与有丝分裂纺锤体的稳定,因此秋水仙碱对微管聚合的抑制将妨碍七叶苷 14 维护纺锤体装置完整性的功能。

Vinblastine

865-21-4sc-491749
sc-491749A
sc-491749B
sc-491749C
sc-491749D
10 mg
50 mg
100 mg
500 mg
1 g
¥1128.00
¥2595.00
¥5077.00
¥19349.00
¥32718.00
4
(0)

长春花碱与微管蛋白结合并抑制微管的形成。由于Septin 14参与细胞分裂过程中微管依赖性过程,长春花碱对微管组装的抑制会破坏Septin 14在细胞分裂和细胞质分裂中的作用。

Griseofulvin

126-07-8sc-202171A
sc-202171
sc-202171B
5 mg
25 mg
100 mg
¥936.00
¥2437.00
¥6611.00
4
(2)

灰黄霉素通过与微管蛋白结合并干扰其聚合来破坏微管功能。这种作用会破坏微管蛋白14在细胞分裂期间正常发挥功能所需的微管蛋白的稳定性,从而抑制微管蛋白14。

Epothilone B, Synthetic

152044-54-7sc-203944
2 mg
¥1986.00
(0)

埃博霉素B与微管蛋白结合,导致微管蛋白稳定,这与紫杉醇非常相似。这种稳定作用会破坏微管蛋白的正常动态,从而抑制Septin 14,而微管蛋白的正常动态对于Septin 14在细胞分裂和胞质分裂过程中的功能至关重要。