AP1S2_Ap1s2 Inhibitors
AP1S2 inhibitors are chemical compounds that directly or indirectly influence the function of AP1S2, a subunit of the adaptor protein complex 1, which is involved in clathrin-coated vesicle assembly and intracellular trafficking. Compounds such as Brefeldin A, Dynasore, Exo1, and Pitstop 2 act by disrupting protein transport and vesicle formation, thereby indirectly impeding the assembly and function of vesicles involving AP1S2. For instance, Brefeldin A inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus, which is a critical step in vesicle assembly, while Dynasore disrupts vesicle formation by inhibiting the GTPase dynamin. Exo1, on the other hand, inhibits the function of the exocyst complex, a key component in vesicle trafficking, thereby decreasing the functional activity of AP1S2.
Compounds like Monensin, Nocodazole, Wortmannin, LY294002, Vinblastine, Genistein, Chlorpromazine, and Latrunculin B influence the function of AP1S2 by disrupting various aspects of intracellular trafficking and signaling. Monensin, for example, disrupts intracellular trafficking by altering ion gradients, while Nocodazole and Vinblastine disrupt vesicle transport along microtubules by depolymerizing microtubules and inhibiting microtubule dynamics, respectively. Wortmannin and LY294002 are PI3K inhibitors that disrupt vesicle trafficking by inhibiting the PI3K-dependent pathway. Genistein is a tyrosine kinase inhibitor that disrupts intracellular signaling, which can indirectly influence vesicle formation and trafficking. Chlorpromazine, a cationic amphiphilic drug, and Latrunculin B, a toxin that binds to actin monomers, inhibit clathrin-mediated endocytosis and actin polymerization respectively, leading to decreased functional activity of AP1S2.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $30.00 $52.00 $122.00 $367.00 | 25 | |
Brefeldin A is a fungal metabolite that inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus. AP1S2 is a subunit of the adaptor protein complex 1 involved in clathrin-coated vesicle assembly. By inhibiting protein transport, Brefeldin A can indirectly impede the assembly and function of vesicles involving AP1S2. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $87.00 | 44 | |
Dynasore is an inhibitor of dynamin, a GTPase involved in vesicle formation. The inhibition of dynamin can disrupt the formation and release of clathrin-coated vesicles from the membrane, a process in which AP1S2 plays a crucial role, leading to decreased functional activity of AP1S2. | ||||||
Exo1 | 461681-88-9 | sc-200752 sc-200752A | 10 mg 50 mg | $82.00 $291.00 | 4 | |
Exo1 is an inhibitor of exocyst complex function. AP1S2 is involved in vesicle trafficking, and the inhibition of the exocyst complex by Exo1 can disrupt this process, thereby decreasing the functional activity of AP1S2. | ||||||
Pitstop 2 | 1419320-73-2 | sc-507418 | 10 mg | $360.00 | ||
Pitstop 2 inhibits clathrin-mediated endocytosis. Given that AP1S2 is involved in clathrin-coated vesicle assembly, the inhibition of clathrin-mediated endocytosis by Pitstop 2 can result in decreased functional activity of AP1S2. | ||||||
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $152.00 $515.00 | ||
Monensin is a sodium ionophore that disrupts intracellular trafficking by altering ion gradients. As AP1S2 is involved in vesicle trafficking, the alteration of ion gradients by Monensin can lead to decreased functional activity of AP1S2. | ||||||
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 is a microtubule-depolymerizing agent. As AP1S2 is involved in vesicle transport along microtubules, the depolymerization of microtubules by Nocodazole can disrupt the transport process, leading to decreased functional activity of AP1S2. | ||||||
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $66.00 $219.00 $417.00 | 97 | |
Wortmannin is a PI3K inhibitor that can disrupt vesicle trafficking by inhibiting the PI3K-dependent pathway. As AP1S2 is involved in vesicle trafficking, the inhibition of PI3K by Wortmannin can lead to decreased functional activity of AP1S2. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $121.00 $392.00 | 148 | |
LY294002 is a PI3K inhibitor that can disrupt vesicle trafficking by inhibiting the PI3K-dependent pathway. As AP1S2 is involved in vesicle trafficking, the inhibition of PI3K by LY294002 can lead to decreased functional activity of AP1S2. | ||||||
Vinblastine Sulfate | 143-67-9 | sc-201447 sc-201447A sc-201447B sc-201447C | 10 mg 50 mg 100 mg 1 g | $107.00 $404.00 $550.00 $2200.00 | 9 | |
Vinblastine is a microtubule-disrupting agent that inhibits microtubule dynamics, leading to the disruption of vesicle transport along the microtubules. Since AP1S2 is involved in vesicle transport, the disruption of microtubule dynamics by Vinblastine can lead to decreased functional activity of AP1S2. | ||||||
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $26.00 $92.00 $120.00 $310.00 $500.00 $908.00 $1821.00 | 46 | |
Genistein is a tyrosine kinase inhibitor that can disrupt intracellular signaling, which can indirectly influence vesicle formation and trafficking. As AP1S2 is involved in vesicle trafficking, the inhibition of tyrosine kinase by Genistein can lead to decreased functional activity of AP1S2. | ||||||