Date published: 2025-10-11

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LYRM4 Activators

Chemical activators of LYRM4 can enhance its function by various biochemical mechanisms. Coenzyme Q10, a vital component in the electron transport chain, can augment the functional activity of LYRM4 by increasing the requirement for properly assembled iron-sulfur clusters, which are crucial for mitochondrial electron transport. Similarly, Methylene Blue serves as an alternative electron acceptor within this chain, thereby increasing the demand for iron-sulfur clusters and, consequently, the activity of LYRM4. Sulfasalazine operates by inhibiting NF-kB, and this action can lead to an increase in mitochondrial function and biogenesis, which in turn heightens the need for LYRM4's role in iron-sulfur cluster assembly. Alpha-lipoic acid, a mitochondrial antioxidant, can support LYRM4 activity by aiding in the repair of oxidative damage and enhancing mitochondrial function, which promotes the assembly of iron-sulfur clusters.

Additional chemicals that activate LYRM4 include precursors and substrates involved in mitochondrial metabolism and iron-sulfur cluster assembly. 5-Aminolevulinic acid, a precursor in heme synthesis, can increase the demand for iron-sulfur cluster assembly, thereby enhancing LYRM4 activity due to its role in synthesizing these clusters for heme-containing proteins. Copper(II) sulfate, as a cofactor, can enhance the activity of enzymes requiring iron-sulfur clusters, indirectly elevating LYRM4 function. N-Acetylcysteine contributes to maintaining an optimal redox state within the mitochondria, essential for LYRM4 activity. Nicotinamide adenine dinucleotide (NAD+) boosts redox reactions, activating LYRM4-dependent processes. Succinic acid, a substrate for succinate dehydrogenase that contains iron-sulfur clusters, can raise LYRM4 activity by increasing substrate availability. Amino acids such as leucine stimulate mitochondrial biogenesis, which then enhances the demand for LYRM4's activity. Pyruvate, a key metabolite, can escalate mitochondrial activity, consequently increasing the requirement for LYRM4. Lastly, retinoic acid, by affecting gene expression and cell differentiation, can elevate mitochondrial biogenesis and function, thus increasing LYRM4 activity in iron-sulfur cluster assembly.

SEE ALSO...

Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Coenzyme Q10

303-98-0sc-205262
sc-205262A
1 g
5 g
$70.00
$180.00
1
(1)

Coenzyme Q10 is involved in electron transport chain. LYRM4 is a component of the iron-sulfur cluster assembly, which is essential for mitochondrial electron transport. Coenzyme Q10 activation enhances electron transport and can thus increase the functional activity of LYRM4 by increasing the demand for properly assembled iron-sulfur clusters.

Sulfasalazine

599-79-1sc-204312
sc-204312A
sc-204312B
sc-204312C
1 g
2.5 g
5 g
10 g
$60.00
$75.00
$125.00
$205.00
8
(1)

Sulfasalazine is a known inhibitor of NF-kB, a transcription factor that regulates immune response. Inhibition of NF-kB can lead to compensatory upregulation of mitochondrial function and biogenesis, which would increase the demand for LYRM4's role in the assembly of iron-sulfur clusters necessary for mitochondrial respiration.

Copper(II) sulfate

7758-98-7sc-211133
sc-211133A
sc-211133B
100 g
500 g
1 kg
$45.00
$120.00
$185.00
3
(1)

Copper(II) sulfate can act as a cofactor for enzymes that require copper for their activity. As LYRM4 is involved in the biosynthesis of iron-sulfur clusters, the presence of copper can enhance the activity of enzymes that require these clusters, indirectly increasing the functional activity of LYRM4.

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 acts as an alternative electron acceptor in the mitochondrial electron transport chain. By facilitating electron transport, it can increase the demand for functional iron-sulfur clusters, thus potentially enhancing the activity of LYRM4 in the assembly of these clusters.

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 for glutathione, an antioxidant that helps maintain the redox state within the mitochondria. An optimal redox state is essential for the function of iron-sulfur cluster enzymes. Therefore, N-Acetylcysteine could enhance the function of LYRM4 by maintaining the environment necessary for its activity.

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)

Alpha-lipoic acid is an antioxidant that is also involved in mitochondrial bioenergetics and can participate in the repair of oxidative damage. It can support LYRM4 activity by improving mitochondrial function and promoting the demand for iron-sulfur cluster assembly.

NAD+, Free Acid

53-84-9sc-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
$56.00
$186.00
$296.00
$655.00
$2550.00
$3500.00
$10500.00
4
(2)

NAD+ is a coenzyme critical for redox reactions in the electron transport chain. By increasing NAD+ levels, LYRM4-dependent iron-sulfur cluster assembly processes are activated to meet the heightened metabolic demands.

Succinic acid

110-15-6sc-212961B
sc-212961
sc-212961A
25 g
500 g
1 kg
$44.00
$74.00
$130.00
(0)

Succinic acid is a substrate for succinate dehydrogenase, which contains iron-sulfur clusters. By increasing substrate availability, LYRM4 activity can be enhanced to support the increased turnover rate of iron-sulfur clusters.

L-Leucine

61-90-5sc-364173
sc-364173A
25 g
100 g
$21.00
$61.00
(0)

Leucine has been shown to stimulate mitochondrial biogenesis through the mTOR pathway. Increased mitochondrial biogenesis would increase the demand for iron-sulfur cluster assembly, thereby activating LYRM4.

Pyruvic acid

127-17-3sc-208191
sc-208191A
25 g
100 g
$40.00
$94.00
(0)

Pyruvate is a key metabolite in cellular respiration and its presence can increase mitochondrial activity. This can lead to increased demand for iron-sulfur clusters, which LYRM4 helps to assemble, thus indirectly activating LYRM4.