ARHGAP25 Activators
Chemical activators of ARHGAP25 play a pivotal role in modulating its function as a GTPase-activating protein. GTP, by binding directly to ARHGAP25, activates its catalytic ability to enhance the hydrolysis of GTP on Rho family GTPases. This action is essential for the inactivation of Rho GTPases, switching them from their active GTP-bound states to inactive GDP-bound forms, thereby regulating various cellular processes. Similarly, GTPγS, a non-hydrolyzable GTP analog, binds to GTPases, resulting in the stabilization of their active forms. This stabilization allows ARHGAP25 to exhibit its GAP activity more robustly as it interacts with these persistently active Rho GTPases. Furthermore, the presence of MgCl2 is crucial for the optimal activity of ARHGAP25, as Mg2+ ions are required cofactors for the action of GTPases, hence facilitating the interaction between Rho GTPases and ARHGAP25.
In addition to these nucleotide-based activators, lipid-derived molecules also contribute to the regulation of ARHGAP25 activity. Phosphatidylinositol 3,4,5-trisphosphate, with its ability to bind to the pleckstrin homology domain of ARHGAP25, can recruit the protein to the plasma membrane, where it interacts with membrane-associated Rho GTPases. This translocation is pivotal in positioning ARHGAP25 in close proximity to its substrates, effectively enhancing its GAP activity. Similarly, sphingosine-1-phosphate and lysophosphatidic acid can activate Rho GTPases, thereby increasing the available pool of active GTPases for ARHGAP25 to act upon. Protein kinase C activators, such as phorbol 12-myristate 13-acetate, phosphorylate components of the Rho GTPase signaling pathways, which can indirectly enhance the interaction of Rho GTPases with ARHGAP25. Additionally, the protection of ARHGAP25 from proteolytic inactivation is afforded by calpeptin, an inhibitor of calpain, which might otherwise cleave and deactivate GAPs, including ARHGAP25. Lastly, ionomycin raises intracellular calcium levels, which, through a cascade of calcium-mediated signaling events, can also facilitate the activation of Rho GTPases, thereby supporting the GAP function of ARHGAP25. Each of these chemicals, through distinct molecular mechanisms, ensures the precise regulation of ARHGAP25, enabling it to maintain cellular homeostasis by controlling the activity of Rho GTPases.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Guanosine-5′-Triphosphate, Disodium salt | 86-01-1 | sc-507564 | 1 g | $714.00 | ||
GTP binds directly to ARHGAP25 and activates its GTPase-activating protein (GAP) function, which enhances the hydrolysis of GTP bound to Rho family GTPases, thus functionally activating ARHGAP25. | ||||||
Farnesyl pyrophosphate ammonium salt | 13058-04-3 | sc-200847 sc-200847A | 1 mg 5 mg | $478.00 $1977.00 | ||
Farnesyl pyrophosphate is a substrate for protein prenylation, a process that can modify proteins like Rho GTPases, which are known substrates for ARHGAP25 GAP activity. Prenylation of Rho GTPases may enhance their interaction with ARHGAP25, leading to increased activation of ARHGAP25's GAP function. | ||||||
Geranylgeranylpyrophosphate triammonium salt | 6699-20-3 | sc-200849 | 200 µg | $122.00 | ||
Geranylgeranyl pyrophosphate, similar to farnesyl pyrophosphate, is involved in the prenylation of proteins such as Rho GTPases. This modification can facilitate the interaction of Rho GTPases with ARHGAP25, leading to increased GAP activity of ARHGAP25. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $28.00 $35.00 $48.00 $125.00 | 2 | |
MgCl2 is a cofactor required for the activity of many enzymes, including those involved in GTPase activity. By binding to Rho GTPases, Mg2+ ions can promote the interaction with ARHGAP25, thus enhancing its GAP activity. | ||||||
Guanosine 5′-O-(3-thiotriphosphate) tetralithium salt | 94825-44-2 | sc-202639 | 10 mg | $465.00 | ||
GTPγS is a non-hydrolyzable analog of GTP which binds to GTPases irreversibly and can serve as a potent activator of GTPase-activating proteins like ARHGAP25 by stabilizing the GTP-bound form of Rho GTPases and allowing ARHGAP25 to exhibit its GAP activity on these GTP-bound forms. | ||||||
D-erythro-Sphingosine-1-phosphate | 26993-30-6 | sc-201383 sc-201383D sc-201383A sc-201383B sc-201383C | 1 mg 2 mg 5 mg 10 mg 25 mg | $165.00 $322.00 $570.00 $907.00 $1727.00 | 7 | |
Sphingosine-1-phosphate has been shown to activate Rho GTPases and may subsequently enhance the activity of ARHGAP25 by increasing the pool of active Rho GTPases that ARHGAP25 can act upon. | ||||||
Lysophosphatidic Acid | 325465-93-8 | sc-201053 sc-201053A | 5 mg 25 mg | $98.00 $341.00 | 50 | |
Lysophosphatidic acid activates Rho GTPases and could lead to an increased interaction with ARHGAP25, thereby enhancing ARHGAP25's GAP activity. | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $41.00 $132.00 $214.00 $500.00 $948.00 | 119 | |
Phorbol esters like phorbol 12-myristate 13-acetate (PMA) activate protein kinase C (PKC), which can phosphorylate various proteins within the Rho GTPase signaling pathways, potentially leading to enhanced interaction between Rho GTPases and ARHGAP25, thereby promoting ARHGAP25's GAP activity. | ||||||
Calpeptin | 117591-20-5 | sc-202516 sc-202516A | 10 mg 50 mg | $121.00 $456.00 | 28 | |
Calpeptin is a known inhibitor of calpain, a protease that can cleave and inactivate Rho GTPase-activating proteins. Inhibition of calpain by calpeptin may protect ARHGAP25 from proteolytic cleavage, thus maintaining its functional activity. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $78.00 $270.00 | 80 | |
Ionomycin is a calcium ionophore that increases intracellular calcium levels, which can activate proteins like calmodulin. Activated calmodulin can interact with various signaling pathways, including those involving Rho GTPases, potentially enhancing the activity of ARHGAP25 by increasing the pool of active Rho GTPases. | ||||||