Date published: 2025-9-13

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ZFP963 Activators

Chemical activators of ZFP963 can orchestrate a series of intracellular events leading to its activation through diverse signaling pathways. Forskolin is known to directly activate adenylate cyclase, consequently increasing the intracellular levels of cyclic AMP (cAMP), which is a secondary messenger that activates protein kinase A (PKA). PKA then phosphorylates target proteins, which can include ZFP963, thus activating it. Similarly, IBMX works to inhibit phosphodiesterases, which are enzymes responsible for breaking down cAMP. This inhibition leads to an accumulation of cAMP in the cell, again enabling PKA to phosphorylate and activate ZFP963. Another related compound, Dibutyryl-cAMP, is a stable analog of cAMP that can diffuse into cells and directly activate PKA, leading to the activation of ZFP963 through phosphorylation.

Additionally, phorbol 12-myristate 13-acetate (PMA) is a potent activator of protein kinase C (PKC), which phosphorylates a wide range of target proteins, potentially including ZFP963. Okadaic Acid and Calyculin A are inhibitors of protein phosphatases PP1 and PP2A, respectively. By inhibiting these phosphatases, the phosphorylated state of proteins like ZFP963 is maintained, thereby keeping ZFP963 active. Calcium ionophores such as A-23187 and Ionomycin increase intracellular calcium levels, which activate calcium-dependent kinases capable of phosphorylating ZFP963, thus leading to its activation. Thapsigargin serves to disrupt calcium storage and can lead to the activation of calcium-dependent kinases, which, like the ionophores, would contribute to the phosphorylation and subsequent activation of ZFP963. KN-93, by inhibiting calmodulin-dependent kinase II, can alter signaling pathways, resulting in the activation of ZFP963. Anisomycin activates stress-activated protein kinases that can also target ZFP963 for phosphorylation and activation. Lastly, Chelerythrine, while a PKC inhibitor, can indirectly trigger the activation of other kinases that might compensate for the inhibition of PKC, leading to the phosphorylation and activation of ZFP963.

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