Date published: 2025-9-23

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ZNF364 Activators

Chemical activators of ZNF364 include a variety of compounds that enhance its activity through different cellular mechanisms. Forskolin, for example, is a potent activator of adenylate cyclase, thereby increasing intracellular cAMP levels. The elevation in cAMP acts as a second messenger to activate protein kinase A (PKA), which can then phosphorylate ZNF364, enhancing its DNA-binding activity and thus its functional role in transcriptional regulation. Similarly, Dibutyryl-cAMP, a synthetic analog of cAMP, directly stimulates PKA, leading to the phosphorylation and subsequent activation of ZNF364. Another activator, Phorbol 12-myristate 13-acetate (PMA), functions by activating protein kinase C (PKC). The activation of PKC has been shown to lead to the phosphorylation of substrate proteins, and ZNF364 can be one of such substrates, where phosphorylation by PKC alters its conformation or interactions with other proteins, thereby activating it.

Additionally, Ionomycin and Thapsigargin both raise intracellular calcium levels, which can activate calcium/calmodulin-dependent protein kinases (CaMKs). These kinases have the capability to phosphorylate ZNF364, resulting in its activation. Calyculin A, by inhibiting protein phosphatases 1 and 2A, prevents the dephosphorylation of ZNF364, maintaining it in an active state. Zinc Pyrithione donates zinc ions, which are crucial for maintaining the structural integrity and the active conformation of ZNF364. Spermine NONOate, by releasing nitric oxide, activates guanylate cyclase, increasing cGMP levels, which can subsequently lead to the activation of kinases that phosphorylate and activate ZNF364. Staurosporine at low concentrations has been shown to activate certain kinases, which can lead to the activation of ZNF364 through phosphorylation. Bromo-ADP-ribose can facilitate the ADP-ribosylation of proteins, a post-translational modification that can activate ZNF364 by altering its interaction with DNA and other proteins. Lastly, Okadaic Acid acts as an inhibitor to protein phosphatases, thereby promoting the phosphorylation state of proteins, including ZNF364, resulting in its activation. Each of these chemicals initiates a cascade of intracellular events that culminate in the activation of ZNF364, enabling it to perform its role in the regulation of gene expression.

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