TRAPPC5 Inhibitors
Chemical inhibitors of TRAPPC5 can influence the protein's role in vesicular trafficking through various mechanisms. Wiskostatin, by selectively inhibiting the N-WASP protein, can impact the actin-polymerization process essential for vesicle movement, thus indirectly affecting TRAPPC5-dependent transport pathways. Similarly, Latrunculin B, which binds to actin and prevents its polymerization, can disrupt cytoskeletal dynamics that are crucial for the vesicular transport processes in which TRAPPC5 is involved. ML141, which acts as a selective inhibitor of the Rho family GTPase Cdc42, can influence actin dynamics by altering the GTPase's activity, thereby impacting the vesicle movement and, consequently, TRAPPC5's function.
Furthermore, compounds like Pitstop 2 and Chlorpromazine, which disrupt clathrin-mediated endocytosis, can indirectly inhibit TRAPPC5 by impeding the normal cycling and trafficking of vesicles. Dynasore, an inhibitor of the GTPase activity of dynamin, can affect vesicle scission during endocytosis, potentially leading to a backlog of vesicular traffic that involves TRAPPC5. Brefeldin A, known for its ability to disrupt the Golgi apparatus structure and function, can prevent TRAPPC5 from mediating vesicle fusion and transport, while Ilimaquinone, causing Golgi dispersion, can also hinder the organization of vesicles that TRAPPC5 is meant to process. Exo1, targeting the exocyst complex, can affect vesicle tethering during exocytosis, which is critical for TRAPPC5's function in trafficking. Lastly, SecinH3, which inhibits cytohesins, can impact vesicle formation and sorting, processes that are essential for the proper functioning of TRAPPC5 in vesicular trafficking. Each of these inhibitors can alter the intracellular transport routes and dynamics, thereby indirectly influencing the activity of TRAPPC5.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Wiskostatin | 253449-04-6 | sc-204399 sc-204399A sc-204399B sc-204399C | 1 mg 5 mg 25 mg 50 mg | $48.00 $122.00 $432.00 $812.00 | 4 | |
Wiskostatin is a selective inhibitor of the actin-polymerization motor protein N-WASP. TRAPPC5 is involved in vesicle trafficking processes that depend on actin polymerization for vesicle movement towards the membrane. Inhibition of N-WASP by Wiskostatin could, therefore, disrupt vesicle transport and indirectly inhibit TRAPPC5's functionality in trafficking. | ||||||
Pitstop 2 | 1419093-54-1 | sc-507418 | 10 mg | $360.00 | ||
Pitstop 2 inhibits clathrin-mediated endocytosis. Since TRAPPC5 is part of the trafficking protein particle complex involved in vesicular transport from the Golgi apparatus, inhibition of endocytosis can disrupt the intracellular transport routes and indirectly inhibit TRAPPC5 by preventing normal vesicle cycling and trafficking. | ||||||
Dynamin Inhibitor I, Dynasore | 304448-55-3 | sc-202592 | 10 mg | $87.00 | 44 | |
Dynasore is a small molecule inhibitor of the GTPase activity of dynamin, which is essential for vesicle scission during endocytosis. TRAPPC5's role in vesicle trafficking could be indirectly inhibited by Dynasore, as the disruption of endocytosis can lead to a backlog of vesicular traffic, thereby affecting TRAPPC5's functional role in vesicle movement. | ||||||
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 the structure and function of the Golgi apparatus. Given that TRAPPC5 functions in trafficking between the endoplasmic reticulum and the Golgi, the disruption of the Golgi apparatus by Brefeldin A would indirectly inhibit TRAPPC5 by preventing it from mediating vesicle fusion and transport. | ||||||
Exo1 | 461681-88-9 | sc-200752 sc-200752A | 10 mg 50 mg | $82.00 $291.00 | 4 | |
Exo1 is an inhibitor of the exocyst complex, a component involved in vesicle tethering during exocytosis. Since TRAPPC5 functions in vesicle trafficking, inhibiting exocytosis indirectly inhibits TRAPPC5 by disrupting the overall vesicle transport pathway, which TRAPPC5 is a part of, leading to an inhibition of its transport and tethering functions. | ||||||
ML 141 | 71203-35-5 | sc-362768 sc-362768A | 5 mg 25 mg | $134.00 $502.00 | 7 | |
ML141 is a selective inhibitor of the Rho family GTPase Cdc42. Cdc42 regulates actin polymerization critical for vesicle movement. Inhibition of Cdc42 by ML141 could indirectly inhibit TRAPPC5 by affecting actin dynamics, and thus vesicle movement, which TRAPPC5 is involved in as part of the trafficking protein particle complex. | ||||||
SecinH3 | 853625-60-2 | sc-203260 | 5 mg | $273.00 | 6 | |
SecinH3 inhibits cytohesins, which are ARF-GTPase exchange factors involved in vesicle budding from the Golgi. Since TRAPPC5 is implicated in vesicle trafficking, SecinH3's inhibition of cytohesins could indirectly inhibit TRAPPC5 by impeding vesicle formation, which is a prerequisite for TRAPPC5's role in trafficking. | ||||||
Chlorpromazine | 50-53-3 | sc-357313 sc-357313A | 5 g 25 g | $60.00 $108.00 | 21 | |
Chlorpromazine is known to disrupt clathrin-mediated endocytosis. As TRAPPC5 is involved in vesicular trafficking, the disruption of clathrin-mediated pathways by Chlorpromazine could indirectly inhibit TRAPPC5 by impeding the endocytosis process, which is necessary for the normal function of the protein in vesicle transport. | ||||||
Latrunculin B | 76343-94-7 | sc-203318 | 1 mg | $229.00 | 29 | |
Latrunculin B binds to actin and prevents its polymerization, disrupting cytoskeletal dynamics. As TRAPPC5 is involved in trafficking that relies on the actin cytoskeleton, the inhibition of actin polymerization by Latrunculin B could indirectly inhibit TRAPPC5 by impairing vesicle transport that depends on the integrity of the actin network. | ||||||