ATP9A Inhibitors
Chemical inhibitors of ATP9A can disrupt its function through various mechanisms, each related to the protein's role in vesicular trafficking and membrane dynamics. Monensin, for example, is an ionophore that alters ion gradients across membranes, which are essential for ATP9A's activity in transmembrane ion transport. The disruption of these gradients by Monensin directly hampers ATP9A's ability to maintain ion homeostasis, leading to its functional inhibition. Similarly, Brefeldin A undermines the Golgi apparatus by inhibiting the formation of transport vesicles. ATP9A, being integral to vesicular trafficking, is inhibited when Brefeldin A prevents the formation of vesicles that are crucial for its transport functions. Nocodazole and Cytochalasin D disrupt the cellular cytoskeleton, affecting microtubules and actin filaments, respectively. These structural changes impede the vesicular transport pathways that ATP9A relies on, thereby inhibiting its function.
Further, Dynasore targets the GTPase activity of dynamin, crucial for vesicle scission during endocytosis, a process in which ATP9A is involved. Inhibition of dynamin by Dynasore leads to a blockade in endocytotic vesicle formation, thus inhibiting ATP9A function. Chlorpromazine disrupts clathrin-mediated endocytosis, another pathway essential for ATP9A's role in vesicle formation and trafficking. Tunicamycin, by inhibiting N-linked glycosylation, prevents proper folding and maturation of ATP9A, which is a glycoprotein, thus inhibiting its activity. Niemann-Pick C1 inhibitor and Filipin disrupt cholesterol trafficking and membrane integrity, respectively, which can affect ATP9A's function in vesicle formation due to altered membrane composition. Genistein inhibits tyrosine kinases that phosphorylate proteins involved in the signaling pathways on which ATP9A's function depends, causing its inhibition. Lastly, Omeprazole and Concanamycin A disrupt proton gradients, which are essential for the vesicular trafficking and membrane dynamics that ATP9A mediates. Omeprazole inhibits the H+/K+ ATPase pump, while Concanamycin A specifically targets V-ATPases, leading to an indirect but effective inhibition of ATP9A's associated activities in maintaining ion homeostasis and vesicle acidification.
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Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $152.00 $515.00 | ||
Monensin is an ionophore that disrupts ion gradients across membranes. ATP9A, being an ATPase involved in transmembrane ion transport, requires these gradients to function properly. Monensin's disruption of ion homeostasis can inhibit ATP9A's ability to maintain these gradients and thus its activity. | ||||||
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 disrupts Golgi apparatus function by inhibiting the formation of transport vesicles. ATP9A is involved in vesicular trafficking; thus, the chemical can inhibit ATP9A's function by preventing the transport vesicles that it requires from forming. | ||||||
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 polymerization, affecting vesicular trafficking pathways. As ATP9A is associated with vesicular transport, the disruption of microtubules can inhibit the trafficking routes necessary for ATP9A's function. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D inhibits actin polymerization, which is crucial for maintaining cytoskeletal structure and thus for vesicular trafficking. By inhibiting actin fibers, this compound can hinder vesicle movement, thereby inhibiting ATP9A which relies on vesicular transport. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $87.00 | 44 | |
Dynasore inhibits the GTPase activity of dynamin, which is required for vesicle scission during endocytosis. As ATP9A is implicated in endosomal function, the inhibition of dynamin can inhibit ATP9A's role in endocytosis. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation in the ER. ATP9A is a glycoprotein that may rely on glycosylation for proper folding and function. By preventing glycosylation, Tunicamycin can inhibit ATP9A's maturation and function. | ||||||
Chlorpromazine | 50-53-3 | sc-357313 sc-357313A | 5 g 25 g | $60.00 $108.00 | 21 | |
Chlorpromazine disrupts clathrin-mediated endocytosis. ATP9A's function is related to vesicle formation and trafficking, which can be impaired by the inhibition of clathrin-mediated pathways, thus inhibiting ATP9A's role in these processes. | ||||||
U 18666A | 3039-71-2 | sc-203306 sc-203306A | 10 mg 50 mg | $140.00 $500.00 | 2 | |
Niemann-Pick C1 inhibitor blocks cholesterol trafficking from lysosomes. Since ATP9A is involved in vesicular trafficking, the disruption of cholesterol transport can affect the membrane composition and indirectly inhibit ATP9A's function in vesicle formation and trafficking. | ||||||
Filipin III | 480-49-9 | sc-205323 sc-205323A | 500 µg 1 mg | $116.00 $145.00 | 26 | |
Filipin binds to cholesterol, disrupting lipid rafts and membrane integrity. As ATP9A is involved in vesicular transport and membrane dynamics, the perturbation caused by Filipin can inhibit ATP9A by altering the membranes it interacts with. | ||||||
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 inhibits tyrosine kinases which can phosphorylate substrates involved in vesicular trafficking and membrane dynamics. As ATP9A is implicated in these processes, inhibiting tyrosine kinases can indirectly inhibit ATP9A by disrupting the signaling pathways it relies on. | ||||||