Date published: 2025-9-17

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ZNF879 Activators

Chemical activators of zinc finger protein 879 can directly influence its DNA-binding activity by providing metal ions that are essential for the structural integrity and function of its zinc finger motifs. Zinc chloride is a primary activator that supplies zinc ions, which are core components of the zinc finger domains. These ions bind to the protein's motifs and are crucial for maintaining the structural conformation that is necessary for the protein to engage with DNA molecules actively. Similarly, magnesium chloride can contribute to the activation of zinc finger protein 879 through the provision of magnesium ions, which help in stabilizing the protein structure, ensuring the DNA binding sites are correctly aligned for interaction with genetic material.

Additional metal ions, such as those provided by nickel(II) sulfate, cobalt(II) chloride, copper(II) sulfate, manganese(II) sulfate, and cadmium chloride, can also interact with zinc finger protein 879. These interactions can induce alterations in the protein conformation and potentially replace zinc in its finger motifs, leading to an activated state that facilitates DNA binding. Sodium orthovanadate acts as a phosphatase inhibitor, maintaining phosphorylation states that are conducive to the protein's activation. This preservation of phosphorylation ensures that zinc finger protein 879 remains in an active state, ready to participate in gene regulation. Forskolin, by increasing cAMP levels, and phorbol 12-myristate 13-acetate (PMA), by activating protein kinase C, can initiate a cascade of intracellular events that lead to the phosphorylation and subsequent activation of zinc finger protein 879. Ionomycin's role in raising intracellular calcium levels activates calcium-dependent kinases, which then phosphorylate the protein, enhancing its DNA-binding capability. Lastly, lithium chloride's inhibition of GSK-3 prevents the degradation of proteins, including zinc finger protein 879, thereby sustaining its active form within the cellular environment.

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