Date published: 2025-9-15

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ZFP51 Activators

Chemical activators of ZFP51 can engage various cellular signaling cascades to induce its activation. Forskolin serves as a direct activator of adenylate cyclase, catalyzing the conversion of ATP to cAMP. Elevated cAMP levels can activate protein kinase A (PKA), which is known to phosphorylate a spectrum of cellular proteins, including ZFP51. This cascade ensures that ZFP51 is functionally activated via phosphorylation. Similarly, IBMX, by inhibiting phosphodiesterases that degrade cAMP, effectively raises cAMP concentrations, which indirectly promotes PKA activation and subsequent phosphorylation of ZFP51. In parallel, Phorbol 12-myristate 13-acetate (PMA) operates through the protein kinase C (PKC) pathway, which phosphorylates a range of targets, and can also be implicated in the activation of ZFP51. This activation through PKC is further accentuated by Okadaic Acid, which, by inhibiting protein phosphatases PP1 and PP2A, prevents the dephosphorylation of proteins, indirectly contributing to the maintenance of ZFP51 in an activated state.

Complementing these mechanisms, Anisomycin activates stress-activated MAP kinase pathways, culminating in the phosphorylation and activation of various proteins, which can include the activation of ZFP51. Sodium Orthovanadate also plays a role by inhibiting protein tyrosine phosphatases, potentially leading to an increased state of phosphorylation within the cell that could encompass ZFP51 activation. Calyculin A's inhibition of protein phosphatases similarly elevates the phosphorylation status within the cell, which may include ZFP51. The cAMP pathway is again targeted by Zaprinast and Rolipram, which inhibit PDE5 and PDE4, respectively, resulting in increased cAMP levels that activate PKA and may lead to ZFP51 phosphorylation and activation. Finally, Dibutyryl-cAMP, a synthetic analog of cAMP, directly activates PKA, leading to phosphorylation of downstream proteins, including ZFP51, thus promoting its activation. These chemicals, through their distinct but often converging pathways, ensure the functional activation of ZFP51 by facilitating its phosphorylation state.

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