Date published: 2025-9-17

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ZNF474 Activators

ZNF474 activators operate through a variety of cellular and molecular mechanisms to elevate the functional activity of this zinc finger protein. Some of these mechanisms include the direct stimulation of adenylyl cyclase, leading to increased levels of cAMP within the cell. The rise in cAMP levels activates protein kinase A, which phosphorylates transcription factors that bind to the promoter region of the ZNF474 gene, resulting in its transcriptional upregulation. Additionally, certain analogs of cAMP function to activate PKA, thus bypassing the initial enzymatic step and directly promoting the phosphorylation of transcription factors that enhance the gene's expression. Other activators interact with receptors that modulate gene expression through binding to promoter regions, recruiting coactivators, and subsequently enhancing transcription.

Furthermore, the activity of ZNF474 is influenced by the modulation of the epigenetic landscape. Compounds that inhibit histone deacetylases result in a more open chromatin configuration, which facilitates the access of transcription factors to the DNA and potentially increases the expression of ZNF474. There are also molecules that inhibit DNA methyltransferases, leading to reduced methylation of DNA and the derepression of silenced genes, which includes the gene coding for ZNF474. Other activators function by inhibiting specific kinases or other enzymes such as GSK-3, which can indirectly lead to an increase in the transcription of genes by altering the activity of various transcription factors. Some activators even bind to nuclear hormone receptors and affect transcription of responsive genes, which encompasses the gene for ZNF474, further contributing to the protein's elevated activity.

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