Date published: 2025-12-18

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ZFP68 Activators

Chemical activators of ZFP68 can engage in various interactions that facilitate the protein's structural and functional activation. Zinc, a crucial component for the structural integrity of zinc finger motifs, directly binds to ZFP68, promoting the stabilization of its DNA-binding domains. This interaction is fundamental for the proper configuration of the protein's tertiary structure, allowing it to engage with its DNA targets effectively. Similarly, magnesium ions play a supportive role by enhancing the catalytic activity of ZFP68 if it is associated with enzymatic processes that require divalent cations. Copper(II) sulfate, known for its capacity to bind to metalloproteins, may interact with potential copper-binding domains within ZFP68, prompting the correct folding of the protein, which is essential for its activation.

Further, cobalt(II) chloride can substitute for zinc in specific zinc finger proteins, which could induce a functional conformation in ZFP68. Nickel(II) sulfate, interacting with possible histidine-rich regions within ZFP68, may induce structural modifications that enhance the protein's ability to bind to its targets. Calcium chloride's involvement is distinct, as calcium ions could trigger signaling pathways that lead to the phosphorylation of ZFP68, thereby activating the protein. Sodium selenite's role is tied to maintaining the protein in a reduced state if ZFP68 is involved in managing oxidative stress, while potassium chloride can alter the protein's electrostatic environment, potentially leading to activation. Manganese(II) chloride could act as a cofactor, enabling the activation of ZFP68 if it forms part of an enzyme system dependent on manganese. Cadmium chloride, although generally toxic, can also bind to ZFP68, potentially eliciting an active protein conformation. Lastly, molybdenum(II) chloride and silver nitrate can interact with ZFP68 if it possesses binding sites for these metals, leading to structural changes that activate the protein. These metal ions facilitate a diverse set of structural and catalytic modifications, each contributing to the functional readiness of ZFP68.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Zinc

7440-66-6sc-213177
100 g
$47.00
(0)

Zinc can bind directly to the zinc finger motifs of ZFP68, which are known to require zinc ions for proper structural configuration, resulting in the stabilization and activation of the protein's DNA binding capacity.

Copper(II) sulfate

7758-98-7sc-211133
sc-211133A
sc-211133B
100 g
500 g
1 kg
$45.00
$120.00
$185.00
3
(1)

Copper can interact with proteins that possess metal-binding sites. In the case of ZFP68, if it contains copper-binding domains, copper ions could facilitate the proper folding and activation of its functional conformation.

Cobalt(II) chloride

7646-79-9sc-252623
sc-252623A
5 g
100 g
$63.00
$173.00
7
(1)

Cobalt can replace zinc in certain zinc finger proteins, potentially altering their conformation and activity. If ZFP68 can similarly bind cobalt, this may lead to an alternative conformation that is functionally active.

Calcium chloride anhydrous

10043-52-4sc-207392
sc-207392A
100 g
500 g
$65.00
$262.00
1
(1)

Calcium ions, through their role in signaling cascades, could activate kinases or other enzymes that phosphorylate ZFP68, leading to its activation.

Sodium selenite

10102-18-8sc-253595
sc-253595B
sc-253595C
sc-253595A
5 g
500 g
1 kg
100 g
$48.00
$179.00
$310.00
$96.00
3
(2)

Selenium is a cofactor for certain antioxidant enzymes. If ZFP68 has a role in oxidative stress response, selenium may be required to maintain the protein in a reduced and active state.

Potassium Chloride

7447-40-7sc-203207
sc-203207A
sc-203207B
sc-203207C
500 g
2 kg
5 kg
10 kg
$25.00
$56.00
$104.00
$183.00
5
(1)

Potassium ions can influence the electrostatic environment of proteins and, if ZFP68 is sensitive to such changes, this could lead to its activation through conformational changes.

Manganese(II) chloride beads

7773-01-5sc-252989
sc-252989A
100 g
500 g
$19.00
$30.00
(0)

Manganese ions can act as cofactors for various enzymes. If ZFP68 is part of an enzyme that requires manganese for activation or if it interacts with such enzymes, manganese could play a role in the protein's activation.

Cadmium chloride, anhydrous

10108-64-2sc-252533
sc-252533A
sc-252533B
10 g
50 g
500 g
$55.00
$179.00
$345.00
1
(1)

Cadmium can bind to proteins with metal-binding domains. If ZFP68 can bind cadmium, this could lead to a conformation that is functionally active, although this is typically a toxic interaction and not physiological.

Silver nitrate

7761-88-8sc-203378
sc-203378A
sc-203378B
25 g
100 g
500 g
$112.00
$371.00
$1060.00
1
(1)

Silver ions can interact with proteins, particularly those with metal binding sites. If ZFP68 can bind silver, this interaction may induce a conformational change that results in the activation of the protein, although silver is typically toxic and not used physiologically.