Pet117 Activators
Chemical activators of Pet117 are involved in various biochemical pathways that assist in the activation of this protein, which is essential for the proper function of cytochrome c oxidase (COX). Coenzyme Q10 plays a pivotal role in the mitochondrial electron transport chain by transferring electrons and facilitating the electron flow that drives ATP synthesis. Its presence can help maintain the necessary electron flux to ensure the proper assembly and activity of COX, thereby supporting the activation of Pet117. Similarly, ubiquinol, an electron carrier within the same pathway, ensures the sustained function of COX by conveying electrons, which is crucial for the activation of Pet117. Riboflavin contributes to this process by serving as a precursor for FAD, a cofactor for complex II, which is part of the electron transport chain and supplies electrons that eventually reach COX, where Pet117 is active.
Copper(II) sulfate provides copper ions, which are integral to the COX enzyme as cofactors. The incorporation of these ions is vital for the holoenzyme's assembly, which includes the activation of Pet117. Succinic acid, a component of the tricarboxylic acid (TCA) cycle, generates reducing equivalents like FADH2 and NADH. These molecules donate electrons to the electron transport chain, culminating in the activity of COX and the functional role of Pet117. NADH, in particular, is a primary donor of electrons in this chain, emphasizing its importance in the activation of Pet117. Alpha-lipoic acid, with its antioxidant properties, helps maintain a reducing environment in mitochondria, which supports the correct assembly and function of COX, hence aiding the activation of Pet117. Ascorbic acid and vitamin E act as antioxidants, with ascorbic acid ensuring the reduced state of iron in the heme groups of COX, and vitamin E maintaining the integrity of mitochondrial components, both of which are conditions that favor Pet117 activation. Sodium azide and malonate, while typically acting as inhibitors, can under certain conditions induce a stress response that leads to the upregulation of COX activity, which in turn could enhance the activation of Pet117.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Coenzyme Q10 | 303-98-0 | sc-205262 sc-205262A | 1 g 5 g | $71.00 $184.00 | 1 | |
Coenzyme Q10 assists in electron transport within mitochondria. Pet117 is involved in the assembly of cytochrome c oxidase (COX), and proper electron transport is crucial for the holoenzyme's assembly and function. Coenzyme Q10's role in mitochondrial electron transport can support the proper assembly and function of COX, thereby functionally activating Pet117. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $46.00 $122.00 $189.00 | 3 | |
Copper is a cofactor for cytochrome c oxidase. By providing copper ions, Copper(II) sulfate can facilitate the incorporation of copper into COX, which is a critical step in the assembly and activation of the enzyme complex where Pet117 functions. | ||||||
Succinic acid | 110-15-6 | sc-212961B sc-212961 sc-212961A | 25 g 500 g 1 kg | $45.00 $75.00 $133.00 | ||
Succinic acid participates in the tricarboxylic acid (TCA) cycle, which generates FADH2 and NADH. These reducing equivalents are used in the electron transport chain where cytochrome c oxidase is the terminal enzyme. The proper function of the TCA cycle can ensure a supply of electrons for the COX assembly and activation, which Pet117 is known to be involved in. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $46.00 | 5 | |
Ascorbic acid can donate electrons to maintain iron in its reduced state. Iron is an integral part of the heme groups in cytochrome c oxidase. Maintaining iron in its reduced state is necessary for proper COX function, thus ascorbic acid can contribute to the activation of Pet117 by ensuring the proper function of its associated holoenzyme. | ||||||
(+)-α-Tocopherol | 59-02-9 | sc-214454 sc-214454A sc-214454B sc-214454C | 10 g 25 g 100 g 1 kg | $43.00 $62.00 $141.00 $430.00 | ||
Vitamin E functions as an antioxidant, protecting cellular components from oxidative damage. By preserving the integrity of mitochondrial membranes and the components of the electron transport chain, Vitamin E can support the function of cytochrome c oxidase, indirectly contributing to the activation of Pet117. | ||||||
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 | $69.00 $122.00 $212.00 $380.00 $716.00 | 3 | |
Alpha-lipoic acid is a cofactor for mitochondrial enzymes and has antioxidant properties. It can help maintain a favorable redox state in mitochondria, which is critical for the assembly and function of cytochrome c oxidase, thereby supporting the activation of Pet117. | ||||||
NAD+, Free Acid | 53-84-9 | sc-208084B sc-208084 sc-208084A sc-208084C sc-208084D sc-208084E sc-208084F | 1 g 5 g 10 g 25 g 100 g 1 kg 5 kg | $57.00 $191.00 $302.00 $450.00 $1800.00 $3570.00 $10710.00 | 4 | |
NADH is a primary electron donor in the electron transport chain, which is necessary for the activation of cytochrome c oxidase. By contributing electrons, NADH supports the electron transport chain, thus aiding in the activation of Pet117. | ||||||
Riboflavin | 83-88-5 | sc-205906 sc-205906A sc-205906B | 25 g 100 g 1 kg | $41.00 $112.00 $525.00 | 3 | |
Riboflavin is a precursor for FAD, a cofactor for complex II in the electron transport chain. The function of complex II is linked to the supply of electrons to the electron transport chain, which culminates in the activation of COX where Pet117 operates. | ||||||
Sodium azide | 26628-22-8 | sc-208393 sc-208393B sc-208393C sc-208393D sc-208393A | 25 g 250 g 1 kg 2.5 kg 100 g | $43.00 $155.00 $393.00 $862.00 $90.00 | 8 | |
Sodium azide is known to inhibit cytochrome c oxidase; however, at sub-inhibitory concentrations, it can upregulate COX activity as a stress response, which could lead to the functional activation of Pet117 by promoting the assembly and activity of COX as a compensatory mechanism. | ||||||