Rootletin Inhibitors
Chemical inhibitors of Rootletin, given the protein's role in ciliogenesis and as a structural component of ciliary rootlets, primarily target cellular processes and pathways involved in microtubule and actin dynamics. These inhibitors do not directly target Rootletin; instead, they modulate the cellular environment and the processes Rootletin is involved in, thereby indirectly influencing its function. Microtubule-targeting agents such as colchicine, nocodazole, paclitaxel, vinblastine, taxol, and monastrol play a significant role in this category. These compounds disrupt microtubule polymerization or stabilization, crucial aspects of ciliogenesis, a process where Rootletin is fundamentally involved. By altering microtubule dynamics, these chemicals indirectly inhibit Rootletin's ability to maintain ciliary structure, thereby impacting cilia formation and function. For instance, colchicine and nocodazole depolymerize microtubules, while taxol stabilizes them, both leading to disrupted microtubule dynamics necessary for ciliary rootlet formation and stability.
On the other hand, compounds targeting actin dynamics, such as cytochalasin D, latrunculin A, swinholide A, and jasplakinolide, inhibit Rootletin by disrupting actin structures essential for ciliogenesis. Actin dynamics are crucial for the formation and maintenance of cilia, and by impairing these structures, these inhibitors indirectly affect Rootletin's function in ciliary rootlets. Furthermore, compounds like blebbistatin and nilotinib, which inhibit myosin II and impact cytoskeletal dynamics, respectively, also play a role in indirectly inhibiting Rootletin. These chemicals affect the broader cytoskeletal dynamics and signaling pathways that are crucial for the proper functioning of cilia, thereby impacting Rootletin's role in ciliary structure and formation. Collectively, these chemical inhibitors of Rootletin highlight the intricate relationship between cytoskeletal dynamics, ciliogenesis, and Rootletin's function. By targeting microtubule and actin dynamics, as well as other aspects of cytoskeletal organization and signaling pathways, these inhibitors can modulate Rootletin's role in ciliary structure and formation.
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| 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 | $100.00 $321.00 $2289.00 $4484.00 $18207.00 $34749.00 | 3 | |
Colchicine disrupts microtubule polymerization, a crucial process in ciliogenesis where Rootletin is involved. By destabilizing microtubules, colchicine can indirectly inhibit Rootletin's function in structuring and stabilizing ciliary rootlets, thus impacting cilia formation and maintenance. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $59.00 $85.00 $143.00 $247.00 | 38 | |
Nocodazole is a microtubule-depolymerizing agent. Given that Rootletin is essential for ciliary rootlet stability, nocodazole's disruption of microtubules can indirectly inhibit Rootletin's ability to maintain ciliary structure, affecting ciliogenesis. | ||||||
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 | $41.00 $74.00 $221.00 $247.00 $738.00 $1220.00 | 39 | |
Taxol stabilizes microtubules, which can paradoxically disrupt microtubule dynamics necessary for ciliogenesis. This stabilization can interfere with Rootletin's function in ciliary rootlet formation, indirectly inhibiting its role in cilia structure and function. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D inhibits actin polymerization. Since actin dynamics are essential for ciliogenesis, this compound can indirectly inhibit Rootletin by disrupting actin structures crucial for the formation and maintenance of cilia. | ||||||
Vinblastine | 865-21-4 | sc-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 | |
Vinblastine interferes with microtubule assembly. By impairing microtubule formation, vinblastine can indirectly inhibit Rootletin's function in ciliary rootlets and impact cilia stability and formation. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds to actin monomers, preventing polymerization. This disruption of actin dynamics can indirectly inhibit Rootletin's role in cilia since proper actin organization is crucial for ciliogenesis and Rootletin's structural integrity in ciliary rootlets. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $72.00 $265.00 $495.00 $968.00 | ||
(S)-(-)-Blebbistatin inhibits myosin II, a motor protein involved in cytoskeletal dynamics. By affecting myosin II activity, blebbistatin can indirectly impact Rootletin's role in ciliary structure and formation, as proper cytoskeletal dynamics are crucial for ciliogenesis. | ||||||
Swinholide A, Theonella swinhoei | 95927-67-6 | sc-205914 | 10 µg | $135.00 | ||
Swinholide A disrupts actin filaments, thereby affecting actin dynamics. This can indirectly inhibit Rootletin by impairing the actin structures essential for ciliary formation and maintenance, impacting Rootletin's structural role in ciliary rootlets. | ||||||
Monastrol | 254753-54-3 | sc-202710 sc-202710A | 1 mg 5 mg | $120.00 $233.00 | 10 | |
Monastrol specifically inhibits Eg5, a kinesin motor protein involved in microtubule dynamics. By inhibiting Eg5, monastrol can disrupt processes crucial for ciliogenesis, indirectly inhibiting Rootletin's role in ciliary rootlet stability. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide stabilizes actin filaments, which can disrupt normal actin dynamics essential for ciliogenesis. This stabilization can indirectly inhibit Rootletin's function in ciliary rootlets, affecting cilia structure and maintenance. | ||||||