FLJ23152 Inhibitors
Chemical inhibitors of FLJ23152 employ various mechanisms to disrupt the protein's function by targeting the cytoskeletal structures within the cell, specifically microtubules and actin filaments. Microtubule-targeting agents such as Paclitaxel, Colchicine, Vinblastine, Vincristine, Podophyllotoxin, Nocodazole, and Eribulin can inhibit FLJ23152 by either stabilizing or destabilizing microtubules, thus preventing the dynamic changes necessary for its function. Paclitaxel and Eribulin, for instance, stabilize microtubules and hinder their disassembly, which can arrest cellular functions where FLJ23152 is involved. Conversely, Colchicine, Vinblastine, Vincristine, Podophyllotoxin, and Nocodazole disrupt microtubule assembly, leading to the inhibition of FLJ23152 if its role is contingent on microtubule polymerization and dynamics, such as in mitosis or intracellular transport.
In parallel, actin-targeting compounds such as Cytochalasin D, Latrunculin A, Jasplakinolide, and Swinholide A interfere with the actin cytoskeleton, thereby inhibiting FLJ23152 if its activity is actin-dependent. Cytochalasin D and Latrunculin A inhibit the polymerization of actin filaments, affecting cellular processes that rely on the proper formation of the actin cytoskeleton. Jasplakinolide, in contrast, stabilizes actin filaments and can promote their polymerization, which would inhibit FLJ23152 by preventing actin filament disassembly. Swinholide A severs actin filaments, which could also inhibit the function of FLJ23152 by disrupting the structural integrity needed for its associated cellular activities. Each of these chemicals, through its distinct interaction with either microtubules or actin filaments, can inhibit the function of FLJ23152, assuming the protein's activity is closely tied to the dynamics and integrity of these cytoskeletal components.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
Paclitaxel stabilizes microtubules and thereby inhibits their disassembly, which is crucial for mitotic and interphase cellular functions. If FLJ23152 is involved in cell cycle regulation or mitotic spindle formation, paclitaxel-mediated stabilization of microtubules can inhibit the function of FLJ23152 by preventing the dynamic changes required for its role. | ||||||
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 binds to tubulin, inhibiting microtubule polymerization. This action disrupts mitotic spindle formation and other processes that rely on microtubule dynamics. If FLJ23152 operates within these cellular mechanisms, colchicine would inhibit its function by impeding the proper assembly of microtubules necessary for its activity. | ||||||
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 interferes with microtubule assembly, which is integral to mitosis and cell proliferation. This disruption would inhibit FLJ23152 function if it is involved with cell division processes or intracellular transport mechanisms that rely on intact microtubules. | ||||||
Podophyllotoxin | 518-28-5 | sc-204853 | 100 mg | $82.00 | 1 | |
Podophyllotoxin binds to tubulin and inhibits the polymerization of microtubules, leading to cell cycle arrest. If FLJ23152's function is related to processes that depend on microtubule dynamics, such as cell division or vesicle transport, podophyllotoxin would inhibit its function by destabilizing microtubules. | ||||||
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 disrupts microtubule networks by interfering with tubulin polymerization, which can lead to cell cycle arrest. By destabilizing microtubules, nocodazole would inhibit the function of FLJ23152 if it is associated with cellular processes like chromosome segregation or organelle movement. | ||||||
Eribulin | 253128-41-5 | sc-507547 | 5 mg | $865.00 | ||
Eribulin inhibits the growth phase of microtubule dynamics, ultimately leading to mitotic blockade. If FLJ23152 is engaged in cell division or relies on microtubule-based structures, eribulin's action would inhibit the function of FLJ23152 by preventing proper microtubule formation. | ||||||
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 mitotic spindles by interacting with microtubule proteins, which can cause mitotic arrest. If FLJ23152 is involved in mitosis or relies on microtubule integrity, griseofulvin would inhibit its function by compromising the microtubule structures necessary for its proper operation. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D disrupts actin filament polymerization, affecting cell shape, motility, and division. If FLJ23152 is involved in actin-dependent processes, cytochalasin D can inhibit its function by preventing the proper formation of the actin cytoskeleton, which is necessary for various cellular activities. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A binds to actin monomers, inhibiting actin polymerization and thus disrupting the actin cytoskeleton. If FLJ23152's function is actin-dependent, latrunculin A would inhibit the protein by impairing the formation and maintenance of actin filaments that are crucial for its activity. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide stabilizes actin filaments and can induce actin polymerization, affecting cell motility and morphology. If FLJ23152 relies on dynamic changes in the actin cytoskeleton, jasplakinolide would inhibit its function by preventing the disassembly of actin filaments required for its activity. | ||||||