CYB5R3 Activators
CYB5R3 Activators encompass a spectrum of chemical entities that inherently bolster the enzymatic activity of CYB5R3 through distinct mechanisms within cellular biochemistry. Substrates like NADH provide the necessary reducing equivalents that CYB5R3 utilizes to convert cytochrome b5 to its reduced form, a process foundational for numerous electron transfer reactions across various metabolic pathways. Riboflavin, serving as a precursor to the FAD cofactor, is indispensable for CYB5R3's functionality, as the flavoprotein nature of CYB5R3 demands a tightly bound FAD molecule to facilitate electron transfer. Menadione and Coenzyme Q10, by shuttling electrons within the cell, indirectly perpetuate the redox cycle that CYB5R3 is integral to, thereby boosting its activity. The antioxidant functions of Vitamin E and Vitamin C are also crucial, as they play a protective role, preserving the heme group of cytochrome b5 in a reduced state, ensuring a continuous and efficient substrate turnover by CYB5R3.
Furthermore, Methylene Blue offers an alternative pathway for electron transfer, effectively complementing the natural electron acceptors of CYB5R3 and potentially optimizing its activity under varied cellular conditions. Nicotinamide contributes to the pool of NAD+, which is a substrate for the reductive actions of CYB5R3, reinforcing its role in electron transfer. The availability of substrates such as L-Arginine and Glucose can indirectly influence the activity of CYB5R3 by modulating the levels of nitric oxide and NADH, respectively, which are instrumental in maintaining CYB5R3's reductive capacity. Succinate, another key metabolite, by participating in the tricarboxylic acid cycle, supports the generation of FADH2, indirectly sustaining a redox state conducive to CYB5R3's function. Collectively, these activators work in concert to ensure that CYB5R3 operates at peak efficiency, thereby maintaining the crucial balance of electron transfer reactions vital for cell survival and function.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Vitamin K3 | 58-27-5 | sc-205990B sc-205990 sc-205990A sc-205990C sc-205990D | 5 g 10 g 25 g 100 g 500 g | $26.00 $36.00 $47.00 $136.00 $455.00 | 3 | |
Menadione (Vitamin K3) functions as a redox-cycling compound that can indirectly increase the electron flux through the CYB5R3 pathway by accepting electrons and then transferring them to oxygen, regenerating oxidized CYB5R3 for further catalytic cycles. | ||||||
Riboflavin | 83-88-5 | sc-205906 sc-205906A sc-205906B | 25 g 100 g 1 kg | $41.00 $112.00 $525.00 | 3 | |
As a precursor of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), riboflavin is essential for the formation of active flavoproteins, which include CYB5R3. Adequate levels of riboflavin enhance the proper functioning of CYB5R3 by ensuring the availability of its cofactors. | ||||||
Hemin chloride | 16009-13-5 | sc-202646 sc-202646A sc-202646B | 5 g 10 g 25 g | $102.00 $160.00 $326.00 | 9 | |
Hemin can induce the synthesis of cytochrome b5, which is the substrate for CYB5R3. By increasing the substrate availability, hemin indirectly enhances the functional activity of CYB5R3. | ||||||
Palmitic Acid | 57-10-3 | sc-203175 sc-203175A | 25 g 100 g | $114.00 $286.00 | 2 | |
Palmitic acid serves as a substrate for fatty acid elongation processes that involve electron transfer reactions mediated by cytochrome b5 and CYB5R3. An increase in fatty acid substrates can enhance the activity of CYB5R3 by increasing its substrate turnover. | ||||||
D-erythro-Sphingosine | 123-78-4 | sc-3546 sc-3546A sc-3546B sc-3546C sc-3546D sc-3546E | 10 mg 25 mg 100 mg 1 g 5 g 10 g | $90.00 $194.00 $510.00 $2448.00 $9384.00 $15300.00 | 2 | |
Sphingosine may act as a modulator of lipid signaling pathways that involve CYB5R3. By influencing the composition of lipid rafts where CYB5R3 is localized, sphingosine could indirectly enhance the protein's functional activity. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $46.00 | 5 | |
Ascorbic acid can donate electrons to regenerate reduced forms of cytochrome b5 and CYB5R3, thus maintaining their activity in electron transfer reactions and enhancing CYB5R3's role in metabolic processes. | ||||||
Iron(II) sulfate solution | 10028-21-4 | sc-224024 | 1 each | $46.00 | ||
By providing a source of ferrous ions, ferrous sulfate can contribute to the synthesis of heme, a component of cytochrome b5. Enhanced heme synthesis could lead to increased CYB5R3 activity due to elevated substrate levels. | ||||||
(+)-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 | ||
α-Tocopherol (Vitamin E) can protect membrane integrity and the redox state of lipid environments where CYB5R3 operates, indirectly maintaining the enzyme's activity by preventing oxidative damage. | ||||||
Coenzyme Q10 | 303-98-0 | sc-205262 sc-205262A | 1 g 5 g | $71.00 $184.00 | 1 | |
Coenzyme Q10 participates in the mitochondrial electron transport chain and can influence the redox state of cells. By maintaining a reduced environment, it may indirectly enhance the activity of CYB5R3 by facilitating electron transfer. | ||||||