Date published: 2025-12-15

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ZNF146 Activators

ZNF146 include a variety of metals and small molecules that can influence the protein's structure and function. Zinc plays a foundational role in the structural integrity of ZNF146, as this protein belongs to the zinc finger protein family. The presence of zinc ions is crucial for the proper folding of ZNF146, enabling it to interact with DNA effectively. Similarly, other metal ions such as magnesium, found in magnesium chloride, are known to affect the conformation of zinc finger domains. Magnesium ions can enhance the DNA-binding capability of ZNF146 by stabilizing its structure. Transition metals like cobalt from cobalt(II) chloride, nickel from nickel(II) sulfate, and copper from copper(II) sulfate can replace zinc in the zinc finger motifs. This substitution can lead to an activated form of ZNF146 due to altered conformational states that may promote DNA binding. Furthermore, cadmium from cadmium chloride can also interact with the zinc finger motifs, potentially leading to the activation of ZNF146 through similar conformational changes.

In addition to metal ions, small molecule inhibitors and activators can also influence ZNF146 activity. Sodium orthovanadate can inhibit phosphatases, maintaining phosphorylation states of proteins that interact with ZNF146, potentially leading to its activation. Forskolin, by elevating cAMP levels, can activate protein kinase A (PKA), which in turn can phosphorylate and activate proteins associated with ZNF146, enhancing its function. DNA methyltransferase inhibitors like 5-azacytidine can alter chromatin structure, thus activating ZNF146 by increasing the accessibility of its DNA binding sites. Histone deacetylase inhibitors such as Trichostatin A and sodium butyrate lead to chromatin remodeling, which can activate ZNF146 by facilitating DNA interaction. Additionally, Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which can phosphorylate regulatory proteins that enhance the activity of ZNF146, contributing to its functional activation within the cell.

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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Zinc

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

ZNF146 is a zinc finger protein; zinc ions can directly enable the proper folding of the protein, hence activating its DNA-binding capability.

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 ions can influence the structural conformation of zinc finger domains in proteins like ZNF146, potentially enhancing their interaction with DNA.

Cobalt(II) chloride

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

Cobalt can replace zinc in zinc finger proteins, potentially altering and activating the DNA-binding activity of ZNF146.

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 bind to zinc finger motifs, potentially activating ZNF146 by inducing conformational changes that affect its function.

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 interact with zinc finger proteins, potentially activating ZNF146 through structural modulation leading to altered DNA binding.

Sodium Orthovanadate

13721-39-6sc-3540
sc-3540B
sc-3540A
5 g
10 g
50 g
$45.00
$56.00
$183.00
142
(4)

Vanadate can act as a phosphatase inhibitor, potentially activating ZNF146 by preventing dephosphorylation of proteins that interact with ZNF146, thus enhancing its function.

Forskolin

66575-29-9sc-3562
sc-3562A
sc-3562B
sc-3562C
sc-3562D
5 mg
50 mg
1 g
2 g
5 g
$76.00
$150.00
$725.00
$1385.00
$2050.00
73
(3)

Forskolin activates adenylyl cyclase increasing cAMP levels, which could lead to the activation of PKA and subsequent phosphorylation and activation of proteins that associate with ZNF146.

5-Azacytidine

320-67-2sc-221003
500 mg
$280.00
4
(1)

As a DNA methyltransferase inhibitor, 5-azacytidine changes chromatin structure and DNA accessibility, potentially activating ZNF146 by increasing its access to DNA binding sites.

Trichostatin A

58880-19-6sc-3511
sc-3511A
sc-3511B
sc-3511C
sc-3511D
1 mg
5 mg
10 mg
25 mg
50 mg
$149.00
$470.00
$620.00
$1199.00
$2090.00
33
(3)

Trichostatin A is a histone deacetylase inhibitor, which can cause chromatin remodeling and potentially activate ZNF146 by enhancing its DNA binding affinity.

Sodium Butyrate

156-54-7sc-202341
sc-202341B
sc-202341A
sc-202341C
250 mg
5 g
25 g
500 g
$30.00
$46.00
$82.00
$218.00
19
(3)

Sodium butyrate acts as a histone deacetylase inhibitor, which may activate ZNF146 by altering chromatin structure to facilitate DNA binding.