Date published: 2025-9-13

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Olr1733 Activators

Chemical activators of Olr1733 employ a variety of mechanisms to modulate the protein's activity. Forskolin acts by directly stimulating adenylyl cyclase, which increases the intracellular levels of cAMP. The elevated cAMP then activates protein kinase A (PKA), a kinase that can phosphorylate Olr1733, leading to its activation. Similarly, Dibutyryl-cAMP and 8-Bromo-cAMP, both membrane-permeable cAMP analogs, elevate intracellular cAMP levels, activating PKA, which may then target Olr1733 for phosphorylation. Ionomycin, serving as a calcium ionophore, increases the intracellular concentration of calcium ions, which activates calmodulin-dependent kinases capable of phosphorylating Olr1733. BAY K8644, as an L-type calcium channel agonist, induces calcium influx and thus could also activate calcium-dependent kinases that phosphorylate Olr1733.

In parallel, Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), another kinase that can phosphorylate Olr1733. Thapsigargin, by inhibiting the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA), raises cytosolic calcium levels, which could activate various calcium-dependent signaling pathways and potentially result in the phosphorylation of Olr1733. Okadaic Acid, targeting protein phosphatases such as PP1 and PP2A, prevents the dephosphorylation of proteins, potentially maintaining Olr1733 in an activated state. Zinc Sulfate, which modulates the activity of various kinases and phosphatases through the manipulation of zinc ion concentrations, may also influence the phosphorylation state of Olr1733. Lastly, Anisomycin activates stress-activated protein kinases like JNK and p38 MAP kinase, which could phosphorylate Olr1733, while Sodium Fluoride inhibits protein phosphatases, potentially leading to the accumulation of phosphorylated Olr1733. Together, these chemicals create an environment conducive to the activation of Olr1733 through direct or indirect influence on kinases and phosphatases that regulate the phosphorylation status of the protein.

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