Date published: 2025-9-15

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Olr556 Activators

Chemical activators of Olr556 utilize various molecular pathways to modulate the protein's activity. Forskolin, by directly activating adenylyl cyclase, raises intracellular cyclic AMP levels, which in turn activate protein kinase A (PKA). PKA is known to phosphorylate a myriad of proteins, and in the case of Olr556, this phosphorylation results in its activation. Similarly, Phorbol 12-myristate 13-acetate (PMA) engages protein kinase C (PKC), another kinase that phosphorylates proteins. The activation of PKC by PMA may lead to the phosphorylation of Olr556, modifying its activity. Ionomycin functions as a calcium ionophore, which increases intracellular calcium concentrations and activates calcium-dependent kinases, potentially leading to the phosphorylation of Olr556. BAY K8644 operates as an L-type calcium channel agonist, also boosting calcium levels within the cell, which can lead to Olr556 activation through calcium-stimulated phosphorylation.

Furthermore, Thapsigargin elevates cytosolic calcium by inhibiting the sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA), which could activate calcium-dependent kinases that phosphorylate Olr556. Ouabain, by inhibiting Na+/K+ ATPase, alters intracellular ion gradients and may activate specific kinases that lead to the phosphorylation of Olr556. Zinc Pyrithione elevates intracellular zinc levels, which can activate zinc-sensitive kinases that then phosphorylate Olr556. Okadaic Acid, a protein phosphatase inhibitor, prevents the dephosphorylation of proteins, potentially leading to sustained activation of Olr556 if it is normally regulated by such phosphatases. Anisomycin activates stress-activated protein kinases (SAPKs), which may phosphorylate Olr556 if it is among their substrates. Veratridine, acting as a sodium channel agonist, could initiate the activation of sodium-sensitive kinases, possibly leading to Olr556 phosphorylation. H-89 Dihydrochloride, as a PKA inhibitor, may induce the activation of alternative kinases that phosphorylate Olr556. Lastly, Calyculin A prevents the dephosphorylation of proteins by inhibiting protein phosphatases like PP1 and PP2A, which may result in the maintenance of Olr556 in a phosphorylated, active state.

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