Date published: 2025-10-29

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Olr482 Activators

Chemical activators of Olr482 can engage in a variety of molecular interactions to promote the protein's activation through different intracellular signaling pathways. Forskolin, for instance, directly stimulates adenylate cyclase, which in turn raises the levels of cAMP within the cell. The increase in cAMP activates protein kinase A (PKA), a kinase that can phosphorylate and activate Olr482. In a related mechanism, Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which is known to phosphorylate target proteins, including potentially Olr482, leading to their activation. Ionomycin, by increasing intracellular calcium levels, can trigger the activation of calcium-dependent protein kinases, which may then phosphorylate and activate Olr482. Similarly, BAY K8644, by acting as an L-type calcium channel agonist, causes an influx of calcium that could engage Olr482 in calcium-dependent signaling pathways.

Further, Thapsigargin, which inhibits the sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA), leads to an increased cytosolic calcium level, indirectly promoting the activation of calcium-mediated signaling that can involve Olr482. Ouabain's inhibition of the Na+/K+ ATPase might indirectly lead to elevated intracellular calcium concentrations, which could activate Olr482. Zinc pyrithione increases intracellular zinc levels, which can activate signaling pathways involving Olr482. Protein phosphatase inhibitors like Okadaic acid and Calyculin A prevent dephosphorylation, thereby maintaining proteins such as Olr482 in a phosphorylated and active state. Anisomycin's activation of stress-activated protein kinases may lead to the downstream activation of Olr482 as part of the cellular stress response. Finally, Veratridine induces sodium influx, potentially leading to the activation of Olr482 through depolarization-activated signaling pathways, while H-89 dihydrochloride, despite being a PKA inhibitor, can induce compensatory cellular responses that activate other kinases, which in turn could lead to Olr482 activation.

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