prefoldin 4 Inhibitors
Chemical inhibitors of prefoldin 4 act primarily through their interactions with microtubules, which are integral to the proper folding and stabilization of nascent polypeptide chains-a fundamental process that prefoldin 4 is involved in. Colchicine, for instance, binds to tubulin and disrupts microtubule polymerization, which can interfere with the role of prefoldin 4 in the folding of new polypeptides. Similarly, Vinblastine and Vincristine, both of which bind to tubulin at different sites, prevent microtubule assembly, thereby potentially leading to functional inhibition of prefoldin 4. Podophyllotoxin and Combretastatin A-4 also target tubulin and inhibit its polymerization, an action which can affect the stability of microtubules and consequently, the function of prefoldin 4. Albendazole acts in a similar manner by inhibiting tubulin polymerization, which can alter the microtubule dynamics essential for prefoldin 4 activity.
Other compounds, such as Paclitaxel and Peloruside A, stabilize microtubules and prevent their disassembly, which can affect the dynamics necessary for prefoldin 4 to assist in proper protein folding. Eribulin, binding to the growing ends of microtubules, can cause sequestration of tubulin into non-functional aggregates, potentially disrupting the normal microtubule dynamics and thus the function of prefoldin 4. Nocodazole disrupts microtubule networks by binding to tubulin and inhibiting polymerization, which can hinder the cellular processes that require microtubule dynamics, including the stabilization of polypeptides by prefoldin 4. Lastly, 2-Methoxyestradiol, by inducing microtubule destabilization through its unique binding to tubulin, can impact the microtubule dynamics on which prefoldin 4 relies for its functional role in protein folding. Each of these chemical inhibitors, through their distinct actions on microtubules, can lead to a functional inhibition of prefoldin 4 by impacting the microtubule structures essential for its role in protein stabilization and folding.
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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 by binding to tubulin, which can hinder the proper folding of newly synthesized polypeptides that prefoldin 4 is responsible for, thus leading to a functional inhibition of this protein's role in the stabilization of nascent polypeptide chains that require correct folding for their function. | ||||||
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 | |
Paclitaxel stabilizes microtubules and prevents their disassembly, which can affect the dynamics necessary for prefoldin 4 to function properly in the folding process of client proteins, resulting in functional inhibition due to the altered cellular microtubule dynamics. | ||||||
Podophyllotoxin | 518-28-5 | sc-204853 | 100 mg | $84.00 | 1 | |
Podophyllotoxin binds to tubulin and inhibits its polymerization, which can lead to a decrease in microtubule assembly. This can indirectly cause a functional inhibition of prefoldin 4 by disrupting the cytoskeletal dynamics and affecting its role in the proper folding of polypeptides. | ||||||
Griseofulvin | 126-07-8 | sc-202171A sc-202171 sc-202171B | 5 mg 25 mg 100 mg | $85.00 $220.00 $598.00 | 4 | |
Griseofulvin disrupts microtubule function by binding to polymerized microtubules and can inhibit mitotic spindle formation, which could result in functional inhibition of prefoldin 4 by altering the microtubule dynamics essential for its role in polypeptide folding and stabilization. | ||||||
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 disrupts microtubule networks by binding to tubulin and inhibiting its polymerization, which can hinder the cellular processes that require microtubule dynamics, including the function of prefoldin 4 in stabilizing and folding polypeptides, leading to its functional inhibition. | ||||||
Eribulin | 253128-41-5 | sc-507547 | 5 mg | $865.00 | ||
Eribulin binds to the growing ends of microtubules, causing sequestration of tubulin into non-functional aggregates. This action can lead to a functional inhibition of prefoldin 4 as it may disrupt the normal microtubule dynamics necessary for prefoldin 4's role in protein folding. | ||||||
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 binding to tubulin, which can inhibit the function of prefoldin 4 by disrupting the microtubule network that is necessary for the protein folding processes in which prefoldin 4 participates. | ||||||
2-Methoxyestradiol | 362-07-2 | sc-201371 sc-201371A | 10 mg 50 mg | $71.00 $288.00 | 6 | |
2-Methoxyestradiol binds to tubulin at a site different from other known tubulin inhibitors and induces microtubule destabilization, which could lead to functional inhibition of prefoldin 4 by impacting the microtubule dynamics that prefoldin 4 relies on for its function in protein folding. | ||||||
Albendazole | 54965-21-8 | sc-210771 | 100 mg | $213.00 | 1 | |
Albendazole disrupts microtubule formation by inhibiting tubulin polymerization, which can lead to functional inhibition of prefoldin 4 by altering the microtubule dynamics that are necessary for its activity in stabilizing nascent protein chains during the folding process. | ||||||