Date published: 2025-12-20

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ZFP692 Activators

Chemical activators of ZFP692 include a variety of metal salts and compounds that interact with the protein, each facilitating activation through distinct biochemical interactions. Zinc acetate directly enhances the DNA binding activity of ZFP692 by binding to its zinc finger domains, which are essential for the protein's interaction with genetic material. Similarly, Cobalt(II) chloride may activate ZFP692 by substituting zinc in the zinc finger motifs, potentially inducing a conformation conducive to DNA binding. Nickel(II) sulfate activates ZFP692 by interacting with histidine residues, which might be essential for the protein's structural integrity, leading to a stabilized active conformation.

Copper(II) sulfate and Cadmium chloride contribute to the activation of ZFP692 by binding to the protein, assuming the existence of copper and cadmium-binding sites, respectively. This binding can induce conformational changes that activate ZFP692. Silver nitrate also activates ZFP692 through binding, suggesting ZFP692 contains sites that can coordinate with silver, which facilitates a change in conformation and activation of the protein. Manganese(II) chloride and Molybdenum(II) chloride serve as cofactors that activate ZFP692 by enabling its enzymatic functions, provided that the protein requires these specific metal ions for activation. These ions help in maintaining the protein's structure or in catalyzing reactions that ZFP692 may facilitate.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Zinc

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

Zinc acetate activates ZFP692 by binding to its zinc finger domains, which are crucial for the DNA binding activity of the protein, thereby directly enhancing its ability to interact with genetic material.

Magnesium chloride

7786-30-3sc-255260C
sc-255260B
sc-255260
sc-255260A
10 g
25 g
100 g
500 g
$27.00
$34.00
$47.00
$123.00
2
(1)

Magnesium chloride serves as a cofactor that can activate ZFP692 by facilitating the structural conformation needed for its catalytic or binding functions, if the protein has enzymatic activity that depends on magnesium ions.

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(II) sulfate can activate ZFP692 if the protein has copper-binding sites, enabling a conformational change that allows for proper function or stabilization of the protein's active state.

Cobalt(II) chloride

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

Cobalt(II) chloride can replace zinc in the zinc finger motifs of ZFP692, which may activate the protein by inducing a conformation that is required for its DNA binding activity.

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)

Sodium selenite can maintain ZFP692 in a reduced state that is necessary for its activation, particularly if ZFP692 has a role in redox homeostasis or in the response to oxidative stress.

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 chloride can activate ZFP692 by altering the ionic environment, which can lead to a conformational change in the protein necessary for its activation.

Manganese(II) chloride beads

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

Manganese(II) chloride may serve as a cofactor that activates ZFP692 by enabling enzymatic functions that require manganese ions.

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 chloride can bind to specific domains of ZFP692, which may lead to conformational changes that activate the protein, assuming that ZFP692 has cadmium-binding sites.

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 nitrate can activate ZFP692 if the protein contains binding sites for silver, facilitating a change in conformation that renders the protein active.