Date published: 2025-10-25

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KRTAP12-2 Inhibitors

Chemical inhibitors of KRTAP12-2 function by targeting its structural integrity and binding interactions, essential for its activity. Dithiothreitol (DTT) disrupts KRTAP12-2 by reducing its disulfide bonds, which are vital for maintaining its tertiary structure. Similarly, N-Ethylmaleimide and Iodoacetamide inhibit KRTAP12-2 by alkylating and carboxyamidomethylating the thiol groups of cysteine residues, respectively, preventing the formation and maintenance of disulfide bridges that are crucial for the protein's conformation and function. Additionally, p-Chloromercuribenzoic acid binds to the thiol groups in cysteine residues, which can impede the structural stability and functionality of KRTAP12-2. The chemical Ebselen further contributes to the inhibition by oxidizing thiol groups and disrupting the correct formation of disulfide bonds in KRTAP12-2, while 5,5'-Dithiobis(2-nitrobenzoic acid), also known as Ellman's reagent, indicates the presence of free thiol groups in KRTAP12-2, suggesting the disruption of its disulfide bonds and associated loss of function.

The inhibition of KRTAP12-2 also involves interference with its interactions and metal ion chelation. Tannic acid inhibits KRTAP12-2 by non-specifically binding to the protein, which could hinder its interaction with other molecules or substrates. Methylene Blue and Phenylarsine Oxide both act to modify the redox state of KRTAP12-2; Methylene Blue through redox cycling that oxidizes thiol groups, and Phenylarsine Oxide through binding to vicinal dithiols, both leading to structural and functional disruption. Oxytetracycline and Cadmium chloride target metal ion interactions; Oxytetracycline chelates metal ions essential for the structural stability of KRTAP12-2, while Cadmium chloride replaces zinc ions in zinc finger domains, which are potentially crucial for KRTAP12-2's structure and activity. Lastly, Lead(II) acetate can inhibit KRTAP12-2 by disrupting protein-DNA interactions necessary for the protein's function, further contributing to the cumulative inhibition of this protein's activity.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

N-Ethylmaleimide

128-53-0sc-202719A
sc-202719
sc-202719B
sc-202719C
sc-202719D
1 g
5 g
25 g
100 g
250 g
$22.00
$68.00
$210.00
$780.00
$1880.00
19
(1)

N-Ethylmaleimide can alkylate the thiol groups of cysteine residues in KRTAP12-2, preventing the formation of disulfide bridges, essential for its structure and function.

α-Iodoacetamide

144-48-9sc-203320
25 g
$250.00
1
(1)

Iodoacetamide can irreversibly modify cysteine residues by carboxyamidomethylation, which can inhibit the proper folding and function of KRTAP12-2.

5,5′-Dithio-bis-(2-nitrobenzoic Acid)

69-78-3sc-359842
5 g
$78.00
3
(3)

5,5'-Dithiobis(2-nitrobenzoic acid), also known as Ellman's reagent, can measure free thiol groups in KRTAP12-2, indicating disruption of its disulfide bonds, which is associated with loss of function.

Ebselen

60940-34-3sc-200740B
sc-200740
sc-200740A
1 mg
25 mg
100 mg
$32.00
$133.00
$449.00
5
(1)

Ebselen can oxidize thiol groups in proteins, which may inhibit the correct disulfide bond formation in KRTAP12-2, necessary for its structural integrity and function.

Gallotannin

1401-55-4sc-202619
sc-202619A
sc-202619B
sc-202619C
sc-202619D
sc-202619E
sc-202619F
1 g
10 g
100 g
250 g
1 kg
2.5 kg
5 kg
$25.00
$36.00
$66.00
$76.00
$229.00
$525.00
$964.00
12
(1)

Tannic acid can non-specifically bind to and precipitate proteins, which might inhibit KRTAP12-2 by physically hindering its interaction with other molecules or substrates.

Methylene blue

61-73-4sc-215381B
sc-215381
sc-215381A
25 g
100 g
500 g
$42.00
$102.00
$322.00
3
(1)

Methylene Blue can act as a redox cycling compound, which can oxidize thiol groups and disrupt the redox state of cysteine-rich proteins such as KRTAP12-2, inhibiting its function.

Phenylarsine oxide

637-03-6sc-3521
250 mg
$40.00
4
(1)

Phenylarsine Oxide can bind to vicinal dithiols, such as those found in KRTAP12-2, leading to the disruption of its structure and inhibition of 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 chloride can bind to and replace zinc ions in zinc finger domains, which could be crucial for the structural stability of KRTAP12-2, resulting in inhibition of its function.

Lead(II) Acetate

301-04-2sc-507473
5 g
$83.00
(0)

Lead(II) acetate can disrupt protein-DNA interactions. If KRTAP12-2 requires such interactions for its function, this binding can inhibit the protein's activity.