VEPH1 Inhibitors
Chemical inhibitors of Vesicular Epithelial Protein Homolog 1 (VEPH1) can disrupt the protein's function through various mechanisms by targeting different aspects of the cellular transport system. Brefeldin A, for example, hampers the ARF GTPase, a pivotal molecule in vesicular trafficking, which can lead to the mislocalization and dysfunction of VEPH1. Similarly, Golgicide A, which inhibits GBF1, another GEF for ARF GTPases, also disrupts the vesicular trafficking processes essential for VEPH1's role. Monensin, by altering ion gradients and pH levels within cells, affects lysosomal acidification and vesicular traffic, indirectly inhibiting VEPH1. The action of Dynasore, which targets dynamin GTPase involved in vesicle scission, can result in the functional inhibition of VEPH1 by impeding endocytosis and vesicular transport, essential processes for VEPH1's proper functioning.
Further disrupting the cytoskeletal infrastructure critical for vesicular transport, Nocodazole and Colchicine target microtubule dynamics essential for VEPH1's transport mechanisms; Nocodazole by destabilizing microtubule polymerization, and Colchicine by binding to tubulin, preventing its polymerization. Cytochalasin D and Latrunculin A disrupt actin filaments, another cytoskeletal component, which can inhibit the movement of vesicles integral to VEPH1's function. ML141, by inhibiting Cdc42, affects cytoskeletal organization and vesicle movement, which are necessary for VEPH1's activity. Exo1 specifically targets components of the exocyst complex, crucial for vesicle tethering and docking, which can inhibit VEPH1 by impairing processes required for its function in membrane fusion. Lastly, SecinH3 inhibits cytohesins, affecting ARF GTPase-mediated vesicle formation and trafficking, thereby disrupting processes crucial for VEPH1's function.
SEE ALSO...
| 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 inhibits ADP-ribosylation factor (ARF), a small GTPase involved in vesicular trafficking. VEPH1 is associated with vesicular transport and membrane fusion. Inhibition of ARF by Brefeldin A can disrupt vesicular trafficking processes, which could impede the proper localization and function of VEPH1. | ||||||
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $152.00 $515.00 | ||
Monensin is an ionophore that disrupts intracellular ion gradients and pH, affecting lysosomal acidification and vesicular traffic. By altering these cellular conditions, Monensin can indirectly inhibit VEPH1 by impairing vesicle-mediated processes required for VEPH1's functionality. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $87.00 | 44 | |
Dynasore is a small molecule that inhibits dynamin, a GTPase involved in the scission of clathrin-coated vesicles from membranes. Since dynamin activity is crucial for endocytosis and vesicular trafficking, Dynasore's inhibition of dynamin can result in the functional inhibition of VEPH1 by disrupting its vesicular transport. | ||||||
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, which is essential for vesicle transport along the cytoskeleton. With microtubules being a key component in vesicular trafficking, the inhibition of their polymerization by Nocodazole can lead to functional inhibition of VEPH1 by obstructing its transport mechanisms. | ||||||
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 vital for maintaining the cytoskeleton and for vesicle movement. The inhibition of actin filaments can thus functionally inhibit VEPH1 by preventing vesicle-mediated processes and potentially disrupting the cytoskeletal organization that supports VEPH1 function. | ||||||
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 and inhibits their polymerization, affecting cytoskeletal dynamics. Disrupting actin filaments can functionally inhibit VEPH1 by impairing the cytoskeleton-dependent processes VEPH1 is involved in, particularly related to vesicle transport and membrane fusion. | ||||||
ML 141 | 71203-35-5 | sc-362768 sc-362768A | 5 mg 25 mg | $134.00 $502.00 | 7 | |
ML141 is a selective inhibitor of Cdc42, a small GTPase involved in actin filament organization. Inhibition of Cdc42 can affect cytoskeletal dynamics and vesicle movement, which can functionally inhibit VEPH1 by disturbing the cytoskeletal support and trafficking machinery necessary for VEPH1's activity. | ||||||
Exo1 | 461681-88-9 | sc-200752 sc-200752A | 10 mg 50 mg | $82.00 $291.00 | 4 | |
Exo1 is an inhibitor of exocyst complex component Exo70, which is involved in targeting vesicles to specific docking sites on the plasma membrane. Inhibiting Exo70 can lead to functional inhibition of VEPH1 by impairing the vesicular trafficking and docking processes critical for VEPH1's function. | ||||||
SecinH3 | 853625-60-2 | sc-203260 | 5 mg | $273.00 | 6 | |
SecinH3 inhibits cytohesins, which are guanine nucleotide exchange factors (GEFs) for ARF GTPases, thereby affecting vesicle formation and trafficking. This inhibition can functionally inhibit VEPH1 by disrupting the ARF-mediated processes that are essential for VEPH1's role in vesicle-mediated cellular functions. | ||||||
Golgicide A | 1005036-73-6 | sc-215103 sc-215103A | 5 mg 25 mg | $187.00 $670.00 | 11 | |
Golgicide A is a specific inhibitor of the Golgi BFA resistance factor 1 (GBF1), a GEF for ARF GTPases. Inhibition of GBF1 by Golgicide A can functionally inhibit VEPH1 by impeding the ARF. | ||||||