TXNDC14 Activators
TXNDC14 employ various mechanisms to enhance the protein's function in maintaining cellular protein homeostasis. Glutathione, a naturally occurring antioxidant, provides reducing equivalents to TXNDC14, which are necessary for the reduction of disulfide bonds in substrate proteins. This action assists in the proper folding and stability of these proteins. Dithiothreitol (DTT) similarly promotes the activation of TXNDC14 by breaking down disulfide bonds within the protein, which can lead to the exposure of TXNDC14's active site. This exposure increases the enzyme's activity in catalyzing thiol-disulfide exchange reactions. β-Mercaptoethanol, another reducing agent, activates TXNDC14 by facilitating the cleavage of disulfide bonds within the protein's substrates, thereby enabling TXNDC14 to perform its chaperone role effectively.
NADPH plays a pivotal role in activating TXNDC14 through its function as a cofactor for thioredoxin reductase. This reductase regenerates the reduced form of thioredoxin domain-containing proteins like TXNDC14, which is essential for their ongoing activity in redox regulation. Selenium dioxide indirectly contributes to the activation of TXNDC14 by enhancing the cellular redox environment, which, in turn, supports the protein's catalytic function. Metal ions such as zinc sulfate and copper(II) sulfate activate TXNDC14 by serving as cofactors for various enzymes and by inducing oxidative stress, respectively, which augments the demand for TXNDC14 activity. Iron(II) sulfate contributes to this process by participating in reactions that create reactive oxygen species, leading to protein oxidation and an increased need for TXNDC14's disulfide bond-reducing ability. Methyl methanethiosulfonate (MMTS) activates TXNDC14 by promoting disulfide bond formation through thiol alkylation, which TXNDC14 must then reduce to maintain protein redox balance. Hydrogen peroxide and lipoic acid further activate TXNDC14 by oxidizing protein thiols, necessitating the reduction of newly formed disulfide bonds by TXNDC14 to restore protein function. In essence, these chemicals collectively ensure that TXNDC14 is proficient at mitigating oxidative stress within the cell by maintaining the redox state of proteins.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Glutathione, reduced | 70-18-8 | sc-29094 sc-29094A | 10 g 1 kg | $76.00 $2050.00 | 8 | |
Glutathione activates TXNDC14 by providing reducing equivalents that can be utilized by thioredoxin domain proteins for the catalysis of disulfide bond reduction in substrate proteins, thereby enhancing their proper folding and stability. | ||||||
β-Mercaptoethanol | 60-24-2 | sc-202966A sc-202966 | 100 ml 250 ml | $88.00 $118.00 | 10 | |
β-Mercaptoethanol activates TXNDC14 by acting as a reducing agent, which can facilitate the reduction of disulfide bonds within the protein’s substrates, thereby promoting the chaperone activity of TXNDC14 in protein folding. | ||||||
β-Nicotinamide adenine dinucleotide phosphate | 53-59-8 | sc-215560 sc-215560A | 100 mg 250 mg | $114.00 $198.00 | ||
NADPH activates TXNDC14 through its role as a cofactor for thioredoxin reductase, which in turn regenerates the reduced form of thioredoxin domain-containing proteins like TXNDC14, thus maintaining their activity in redox regulation. | ||||||
Selenium | 7782-49-2 | sc-250973 | 50 g | $61.00 | 1 | |
Selenium dioxide can activate TXNDC14 indirectly by incorporating into selenoproteins, which can enhance the overall cellular redox environment, supporting the catalytic activity of redox-active proteins like TXNDC14. | ||||||
Arsenic(III) oxide | 1327-53-3 | sc-210837 sc-210837A | 250 g 1 kg | $87.00 $224.00 | ||
Arsenic trioxide can activate TXNDC14 by perturbing cellular redox states, which may necessitate increased activity of redox-regulating proteins like TXNDC14 to maintain protein homeostasis. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc sulfate activates TXNDC14 by acting as a cofactor for numerous enzymes, potentially including those that work cooperatively with TXNDC14 in protein folding pathways, augmenting its protein chaperone activity. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper(II) sulfate activates TXNDC14 indirectly by promoting oxidative stress, which can enhance the demand for redox-regulating proteins like TXNDC14 to protect against misfolding and aggregation of cellular proteins. | ||||||
Iron(II) sulfate solution | 10028-21-4 | sc-224024 | 1 each | $45.00 | ||
Iron(II) sulfate activates TXNDC14 by contributing to Fenton chemistry, which generates reactive oxygen species that can oxidize proteins, thereby increasing the requirement for TXNDC14's activity in reducing disulfide bonds for proper protein folding. | ||||||
Hydrogen Peroxide | 7722-84-1 | sc-203336 sc-203336A sc-203336B | 100 ml 500 ml 3.8 L | $30.00 $60.00 $93.00 | 27 | |
Hydrogen peroxide activates TXNDC14 by oxidizing thiol groups within proteins, which can lead to disulfide bond formation; TXNDC14 then reduces these bonds, thereby restoring the function of affected proteins. | ||||||
α-Lipoic Acid | 1077-28-7 | sc-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 | |
Lipoic acid activates TXNDC14 by undergoing redox cycling within the cell, which can modulate the redox state of protein disulfides and thus necessitate the reductive action of TXNDC14 for proper protein folding and function. | ||||||