ZNF214 can interact with the protein in various ways to enhance its function. Zinc Pyrithione and Pyrithione Sodium operate through direct binding to the zinc finger domains of ZNF214, which are crucial for the protein's ability to interact with DNA. These activators may induce a favorable conformational change that promotes DNA binding, thus activating the protein's role in gene regulation. Similarly, Cadmium Chloride, Cobalt(II) Chloride, and Nickel(II) Sulfate can also interact with the zinc finger motifs. By replacing or mimicking the zinc in these domains, they may alter the structure of ZNF214 in a way that enhances its ability to bind to DNA, thereby activating the protein's regulatory functions.
Chloroquine activates ZNF214 by intercalating into DNA, which could increase the affinity of ZNF214 for DNA, enhancing its gene regulatory activity. In the context of metal ion homeostasis, chemicals like Deferasirox, Disulfiram, and Clioquinol influence the availability and balance of metal ions within the cell. Deferasirox sequesters iron, which can indirectly increase the availability of zinc ions, essential for the activation of ZNF214. Disulfiram binds to copper and can affect its cellular levels, potentially leading to an altered zinc homeostasis that, in turn, activates ZNF214. Clioquinol chelates zinc, potentially increasing the local concentration of this metal ion around the zinc finger domains, and facilitating the activation of ZNF214. Auranofin, through the inhibition of thioredoxin reductase, may induce oxidative stress that leads to changes in metal ion dynamics, thereby influencing the activity of ZNF214. Lastly, Zinc Chloride and Zinc Acetate provide a direct supply of zinc ions, which are indispensable for the structural and functional activation of the zinc finger domains in ZNF214, ensuring its ability to bind DNA and regulate gene expression effectively.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc Pyrithione interacts with ZNF214 by binding to the zinc finger domains, which are known to coordinate zinc ions, leading to an alteration in the conformation of ZNF214 and subsequent activation of its DNA-binding activity. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $69.00 | 2 | |
Chloroquine intercalates into DNA, which can result in an increased binding affinity of zinc finger proteins like ZNF214 to DNA, potentially enhancing its functional activity in gene regulation. | ||||||
Cadmium chloride, anhydrous | 10108-64-2 | sc-252533 sc-252533A sc-252533B | 10 g 50 g 500 g | $56.00 $183.00 $352.00 | 1 | |
Cadmium can replace zinc in zinc finger domains, potentially altering the conformation of ZNF214 and activating its binding to DNA, thereby influencing gene expression patterns. | ||||||
Cobalt(II) chloride | 7646-79-9 | sc-252623 sc-252623A | 5 g 100 g | $64.00 $176.00 | 7 | |
Cobalt can mimic zinc in zinc finger proteins, potentially changing the structure of ZNF214 and activating its function in the cellular context. | ||||||
Deferasirox | 201530-41-8 | sc-207509 | 2.5 mg | $180.00 | 9 | |
Deferasirox chelates iron, which might lead to an indirect increase in available zinc ions, potentially enhancing the activation of zinc finger proteins like ZNF214. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Disulfiram can bind to copper and possibly alter its cellular levels, which may influence the homeostasis of other metal ions like zinc, indirectly leading to the activation of ZNF214 through changes in metal ion availability. | ||||||
Clioquinol | 130-26-7 | sc-201066 sc-201066A | 1 g 5 g | $45.00 $115.00 | 2 | |
Clioquinol chelates zinc and other metal ions, which could lead to an increased local concentration of zinc ions, potentially facilitating the activation of ZNF214 by enhancing its structural stability. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $153.00 $214.00 $4000.00 | 39 | |
Auranofin inhibits thioredoxin reductase, which may lead to oxidative stress and subsequent changes in metal ion homeostasis, potentially activating ZNF214 through altered zinc finger protein dynamics. | ||||||