Chemical inhibitors of cilia and flagella associated protein 69 can disrupt the structural and functional integrity of cilia and flagella by targeting the cytoskeletal components that are crucial for their assembly and maintenance. Colchicine, Nocodazole, Vinblastine, Vincristine, Griseofulvin, Epothilone B, and Taxol are chemicals that directly interact with microtubules, the skeletal framework of cilia and flagella. Colchicine and Nocodazole are known to impede the polymerization of microtubules, thereby preventing the proper assembly of cilia and flagella. Vinblastine and Vincristine, similarly, destabilize microtubules, which leads to a breakdown of the existing microtubule network essential for the structure and function of these organelles. Griseofulvin exerts its inhibitory action by binding to tubulin and interfering with microtubule function. On the other hand, Epothilone B and Taxol stabilize microtubules excessively, thereby hindering the dynamic rearrangement required for normal ciliary and flagellar operation.
The actin cytoskeleton also plays a pivotal role in the function of cilia and flagella associated protein 69, and its disruption can result in the inhibition of this protein's function. Cytochalasin D and Latrunculin B bind to actin filaments and monomers, respectively, leading to the inhibition of actin polymerization which is necessary for proper ciliary and flagellar assembly. Swinholide A severs actin filaments, further contributing to the disintegration of the actin structure required for ciliary and flagellar function. Blebbistatin, by inhibiting myosin II, can prevent the correct trafficking and localization of cilia and flagella associated protein 69 to the ciliary base. Additionally, Monastrol, an inhibitor of the kinesin-5 motor protein, disrupts mitotic spindle formation, which is closely related to the transport mechanisms vital for the function of cilia and flagella associated protein 69, highlighting the complexity of the intracellular transport and its significance in maintaining the functionality of these organelles.
SEE ALSO...
Items 1 to 10 of 11 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Colchicine | 64-86-8 | sc-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 | |
Colchicine disrupts microtubule polymerization, which is essential in cilia and flagella structure and function. By destabilizing microtubules, colchicine can lead to the inhibition of cilia and flagella associated protein 69's role in the assembly or maintenance of these structures. | ||||||
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $40.00 $73.00 $217.00 $242.00 $724.00 $1196.00 | 39 | |
Taxol stabilizes microtubules and prevents their disassembly, which can inhibit the dynamic processes required by cilia and flagella associated protein 69 for proper ciliary and flagellar function. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $58.00 $83.00 $140.00 $242.00 | 38 | |
Nocodazole interferes with microtubule polymerization, similar to colchicine, and can inhibit the function of cilia and flagella associated protein 69 by disrupting the microtubule structures that are crucial for ciliary and flagellar operations. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D disrupts actin filament organization. Since actin dynamics are associated with ciliary function and the proper localization of cilia and flagella associated protein 69, this chemical can inhibit the protein by disrupting the actin-related processes needed for ciliary and flagellar assembly and maintenance. | ||||||
Latrunculin B | 76343-94-7 | sc-203318 | 1 mg | $229.00 | 29 | |
Latrunculin B binds to actin monomers, preventing their polymerization. Inhibition of actin filament assembly can affect the trafficking of cilia and flagella associated protein 69 to the ciliary or flagellar compartment, leading to functional inhibition. | ||||||
Vinblastine | 865-21-4 | sc-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 | |
Vinblastine is a microtubule-destabilizing agent that can inhibit the function of cilia and flagella associated protein 69 by disrupting the microtubule networks that are necessary for cilia and flagella structure and function. | ||||||
Griseofulvin | 126-07-8 | sc-202171A sc-202171 sc-202171B | 5 mg 25 mg 100 mg | $83.00 $216.00 $586.00 | 4 | |
Griseofulvin disrupts microtubule function by binding to tubulin, potentially inhibiting the function of cilia and flagella associated protein 69 through the impairment of microtubule dynamics, which are critical for ciliary and flagellar activities. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $179.00 $307.00 $455.00 $924.00 $1689.00 | 7 | |
Blebbistatin inhibits myosin II, and since myosin II activity is implicated in the trafficking and localization of proteins to the ciliary base, this inhibitor can prevent the proper localization of cilia and flagella associated protein 69, thereby inhibiting its function. | ||||||
Epothilone B, Synthetic | 152044-54-7 | sc-203944 | 2 mg | $176.00 | ||
Epothilone B is a microtubule-stabilizing agent that can inhibit the function of cilia and flagella associated protein 69 by interfering with the microtubule dynamics necessary for cilia and flagella maintenance and function. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A severs actin filaments and inhibits actin polymerization. Since cilia and flagella functions are dependent on the proper organization of actin cytoskeleton, this chemical can inhibit the function of cilia and flagella associated protein 69 by disrupting actin structures that are essential for ciliary and flagellar operations. | ||||||