Date published: 2025-9-12

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ZNF845 Activators

Chemical activators of ZNF845 include a variety of compounds that enhance its activity through different mechanisms within cellular signaling pathways. Phorbol 12-myristate 13-acetate is a potent activator of protein kinase C (PKC), which can phosphorylate ZNF845, leading to its activation. Similarly, Forskolin raises the levels of intracellular cyclic AMP (cAMP), in turn activating protein kinase A (PKA), another kinase that can phosphorylate ZNF845, thereby driving its activation. Ionomycin functions by increasing intracellular calcium concentrations, which activates calcium-dependent kinases capable of phosphorylating ZNF845. Thapsigargin contributes to the activation of ZNF845 by inhibiting the sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA), which causes a rise in cytosolic calcium levels, triggering kinase pathways that phosphorylate and activate ZNF845.

Continuing the list of activators, Calyculin A and Okadaic Acid function by inhibiting protein phosphatases 1 and 2A, leading to a sustained phosphorylation state of proteins including ZNF845, which results in its activation. Anisomycin activates stress-activated protein kinases (SAPKs) which then target and phosphorylate ZNF845. Staurosporine and Bisindolylmaleimide I, while generally known as kinase inhibitors, can under specific conditions activate PKC, leading to the phosphorylation and subsequent activation of ZNF845. Dibutyryl-cAMP, a synthetic analog of cAMP, activates PKA which then phosphorylates ZNF845. H-89, although a PKA inhibitor, can lead to compensatory cellular mechanisms that activate PKA, which in turn activates ZNF845 through phosphorylation. Finally, Epigallocatechin gallate can modulate kinase signaling pathways, thus leading to the activation of kinases that phosphorylate and activate ZNF845, demonstrating the diverse array of chemical interactions that can regulate protein function.

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