Date published: 2025-10-31

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Olr420 Activators

Chemical activators of Olr420 can facilitate its activation through various intracellular signaling pathways and biochemical mechanisms. Calcium chloride and ionomycin are two such activators that operate by altering intracellular calcium levels; calcium chloride by providing a direct source of calcium ions, and ionomycin by acting as a calcium ionophore, effectively transporting calcium ions across cellular membranes. The elevated calcium levels can initiate the activation of Olr420, since it is sensitive to calcium-mediated signaling. Additionally, thapsigargin and BAY K8644 also increase intracellular calcium, but through different mechanisms; thapsigargin by inhibiting the SERCA pump, thus preventing calcium sequestration into the endoplasmic reticulum, and BAY K8644 by activating L-type calcium channels, promoting calcium influx.

Further, zinc pyrithione engages Olr420 activation by raising intracellular zinc levels, which can influence metal ion sensors and transporters linked to Olr420. Forskolin operates through a different pathway, increasing intracellular cAMP, which in turn activates PKA. PKA can then target Olr420 or its regulatory proteins, leading to activation. Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which can also phosphorylate Olr420 or its associated proteins, thereby activating the protein. Okadaic Acid, by inhibiting phosphatases like PP1 and PP2A, can result in heightened phosphorylation states within the cell, which may activate Olr420 if its activity is modulated by phosphorylation. Additionally, compounds such as anisomycin, ouabain, veratridine, and calyculin A can activate Olr420 through their respective effects on stress-activated protein kinases, Na+/K+ ATPase, sodium channel function, and inhibition of protein phosphatases, all leading to altered phosphorylation or ion gradient states that can activate the protein.

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