Date published: 2025-11-1

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TXNDC15 Activators

The group of compounds classified as TXNDC15 activators primarily encompasses molecules that influence the redox state within cells, directly or indirectly supporting the environment necessary for TXNDC15 to function optimally. These molecules can increase the antioxidant capacity of the cell by serving as precursors to major antioxidants, like glutathione, or acting directly to quench reactive oxygen species. For example, compounds such as N-Acetylcysteine and Glutathione raise intracellular levels of glutathione, which plays a pivotal role in maintaining cellular redox balance. This balance is crucial for the proper function of proteins like TXNDC15, which are thought to be involved in the formation of disulfide bonds within the endoplasmic reticulum. The enhanced antioxidant status conferred by these molecules would support the optimal redox conditions TXNDC15 requires to catalyze its enzymatic reactions effectively.

Additionally, molecules that function as chemical chaperones contribute to the proper folding of proteins within the endoplasmic reticulum by alleviating stress associated with protein misfolding. By reducing the burden of misfolded proteins, chemical chaperones such as 4-Phenylbutyric acid and Tauroursodeoxycholic acid ensure that proteins like TXNDC15 are not overwhelmed and can carry out their roles in assisting protein folding more efficiently. The modulation of the cellular redox state through compounds like Selenium dioxide and Alpha-tocopherol further exemplifies the indirect support these molecules provide to TXNDC15. They reinforce the cellular defenses against oxidative stress, thereby preserving the endoplasmic reticulum's environment where TXNDC15 operates. Collectively, these chemicals sustain a cellular milieu that is conducive to the protein folding and redox-regulating activities of TXNDC15, ensuring that its potential enzymatic functions are not hindered by adverse oxidative conditions or excessive protein misfolding within the endoplasmic reticulum.

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Items 1 to 10 of 12 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

N-Acetyl-L-cysteine

616-91-1sc-202232
sc-202232A
sc-202232C
sc-202232B
5 g
25 g
1 kg
100 g
$33.00
$73.00
$265.00
$112.00
34
(1)

N-Acetylcysteine serves as a precursor to glutathione, a critical antioxidant within cells. By elevating intracellular glutathione levels, it can reduce oxidative stress and potentially enhance the protein folding capacity of the endoplasmic reticulum, indirectly supporting the function of TXNDC15 in maintaining the redox environment required for its activity.

Glutathione, reduced

70-18-8sc-29094
sc-29094A
10 g
1 kg
$76.00
$2050.00
8
(2)

Glutathione is the primary antioxidant in cells and plays a significant role in maintaining the redox state. Supplementing cells with glutathione can bolster the endogenous antioxidant systems, facilitating an environment for TXNDC15 to catalyze disulfide bond formation in nascent proteins more efficiently.

α-Lipoic Acid

1077-28-7sc-202032
sc-202032A
sc-202032B
sc-202032C
sc-202032D
5 g
10 g
250 g
500 g
1 kg
$68.00
$120.00
$208.00
$373.00
$702.00
3
(1)

(+)-Lipoic acid is an essential cofactor for mitochondrial enzymes and also exhibits antioxidant properties. By enhancing mitochondrial function and reducing oxidative stress, it can indirectly support TXNDC15 function by maintaining a redox balance in the cell, favoring proper protein folding and disulfide bond formation within the endoplasmic reticulum.

4-Phenylbutyric acid

1821-12-1sc-232961
sc-232961A
sc-232961B
25 g
100 g
500 g
$52.00
$133.00
$410.00
10
(1)

4-Phenylbutyric acid is a chemical chaperone known to reduce endoplasmic reticulum stress. By alleviating misfolded protein load, it can facilitate the proper folding of proteins, in which TXNDC15 is involved, thus indirectly enhancing TXNDC15’s role in assisting protein folding.

Tauroursodeoxycholic Acid, Sodium Salt

14605-22-2sc-281165
1 g
$644.00
5
(1)

Tauroursodeoxycholic acid acts as a chemical chaperone reducing endoplasmic reticulum stress and supports proper protein folding. It can indirectly promote TXNDC15 function by stabilizing the endoplasmic reticulum environment and enhancing the machinery involved in protein disulfide isomerization, a process where TXNDC15 is potentially involved.

Selenium

7782-49-2sc-250973
50 g
$61.00
1
(1)

Selenium is a cofactor for antioxidant enzymes like glutathione peroxidases. Selenium dioxide can enhance these antioxidant systems, indirectly supporting TXNDC15 in maintaining the redox state within the endoplasmic reticulum that is conducive to its role in protein folding.

Curcumin

458-37-7sc-200509
sc-200509A
sc-200509B
sc-200509C
sc-200509D
sc-200509F
sc-200509E
1 g
5 g
25 g
100 g
250 g
1 kg
2.5 kg
$36.00
$68.00
$107.00
$214.00
$234.00
$862.00
$1968.00
47
(1)

Curcumin is a compound known to exert antioxidant effects. It can indirectly affect TXNDC15 by mitigating oxidative stress within cells, thus maintaining an optimal redox state in the endoplasmic reticulum for disulfide bond formation in proteins, a function that TXNDC15 may be associated with.

L-Ascorbic acid, free acid

50-81-7sc-202686
100 g
$45.00
5
(1)

Ascorbic acid is a vitamin that acts as a reducing agent and antioxidant in vivo. It can indirectly facilitate the function of TXNDC15 by contributing to the maintenance of a reduced state within the endoplasmic reticulum, which is necessary for the catalytic activity of proteins involved in disulfide bond formation.

Disulfiram

97-77-8sc-205654
sc-205654A
50 g
100 g
$52.00
$87.00
7
(1)

Disulfiram can modulate the redox state of cells by inhibiting enzymes involved in the metabolism of reactive oxygen species. It can indirectly contribute to the functionality of TXNDC15 by promoting a redox environment that supports protein folding within the endoplasmic reticulum, thereby assisting TXNDC15 in its putative role in this process.

(+)-α-Tocopherol

59-02-9sc-214454
sc-214454A
sc-214454B
10 g
25 g
100 g
$42.00
$61.00
$138.00
(1)

Alpha-tocopherol is an antioxidant vitamin that protects cellular membranes from oxidative damage. By preserving the integrity of the endoplasmic reticulum membrane, it can support the protein folding environment, indirectly facilitating the function of TXNDC15 in oxidative protein folding.