MRP-S35 Activators
hemical activators of MRP-S35 include a variety of inorganic salts and organic compounds that interact with the protein and its associated structures within the mitochondria. Magnesium chloride, manganese(II) chloride, and cobalt(II) chloride can all activate MRP-S35 by stabilizing the mitochondrial ribosome structure, which is essential for its role in protein synthesis. Magnesium ions in particular are crucial for maintaining the integrity of ribosomes. Manganese ions support the function of enzymes involved in mitochondrial energy metabolism, which can lead to an increased demand for mitochondrial proteins and the activation of MRP-S35 to meet this need. Similarly, cobalt ions may substitute for magnesium or calcium, enhancing the stability of mitochondrial ribosomes and thereby activating MRP-S35.
Other activators such as zinc sulfate and copper(II) sulfate can further influence the activity of MRP-S35. Zinc ions are integral to the structural maintenance of proteins and nucleic acids, and their interaction with MRP-S35 can promote proper folding and enhance its functionality within the ribosome. Copper ions facilitate electron transfer reactions, crucial in mitochondrial energy production, potentially increasing the activity of MRP-S35 by enhancing its role in the assembly or function of mitochondrial ribosomes. Iron(II) sulfate's role is similarly supportive as iron is vital for the synthesis of heme-containing proteins and iron-sulfur clusters in mitochondria, hence stimulating the assembly and activity of mitochondrial ribosomes and the activation of MRP-S35. Sodium selenite and ammonium molybdate have roles in enzyme function and metabolism, which can lead to the activation of MRP-S35 by increasing the assembly and function of mitochondrial ribosomes necessary for synthesizing protective and metabolic proteins. Organic compounds like L-Lysine and L-Arginine influence post-translational modifications and nitric oxide synthesis, respectively, which can enhance mitochondrial function and, consequently, the activity of MRP-S35. Lastly, NAD+ and coenzyme Q10 play roles in redox reactions and the electron transport chain, their presence signaling a greater need for mitochondrial ribosomal protein synthesis, leading to the activation of MRP-S35 as it contributes to these essential mitochondrial processes.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $27.00 $34.00 $47.00 $123.00 | 2 | |
Magnesium chloride provides magnesium ions, which are crucial in stabilizing the structure of ribosomes. As MRP-S35 is a mitochondrial ribosomal protein, the presence of magnesium can stabilize the ribosome and therefore enhance the functional activity of MRP-S35 in protein synthesis. | ||||||
Manganese(II) chloride beads | 7773-01-5 | sc-252989 sc-252989A | 100 g 500 g | $19.00 $30.00 | ||
Manganese ions act as cofactors for various enzymes, including those involved in the mitochondrial energy metabolism. Their presence can enhance the function of these enzymes, thus increasing the demand for mitochondrial proteins and thereby activating MRP-S35 to meet the increased need for components of the mitochondrial ribosome. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions are known to play a role in the structural integrity of proteins and nucleic acids. Binding of zinc ions to MRP-S35 can directly activate its function in the mitochondrial ribosome, possibly by promoting proper folding or enhancing interaction with ribosomal RNA or other ribosomal proteins. | ||||||
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 ions can interact with proteins to facilitate electron transfer reactions, which are vital in mitochondrial energy production. This interaction may increase the activity of MRP-S35 by enhancing its role in the assembly or function of mitochondrial ribosomes, which are essential for synthesizing proteins involved in the electron transport chain. | ||||||
Iron(II) sulfate solution | 10028-21-4 | sc-224024 | 1 each | $45.00 | ||
Iron is a critical component of heme-containing proteins and iron-sulfur clusters that are synthesized in mitochondria. The presence of iron can stimulate the assembly and activity of mitochondrial ribosomes, thereby activating MRP-S35 as it contributes to the synthesis of these essential mitochondrial components. | ||||||
Cobalt(II) chloride | 7646-79-9 | sc-252623 sc-252623A | 5 g 100 g | $63.00 $173.00 | 7 | |
Cobalt ions can replace magnesium or calcium in certain biological processes. In the context of MRP-S35, cobalt might enhance the protein's function by stabilizing the mitochondrial ribosome structure, leading to an increased activation of MRP-S35 for effective mitochondrial protein synthesis. | ||||||
Sodium selenite | 10102-18-8 | sc-253595 sc-253595B sc-253595C sc-253595A | 5 g 500 g 1 kg 100 g | $48.00 $179.00 $310.00 $96.00 | 3 | |
Selenium is a cofactor for antioxidant enzymes like glutathione peroxidases. Its presence can lead to the formation of proteins that protect against oxidative damage in mitochondria, which may activate MRP-S35 due to its role in assembling mitochondrial ribosomes that synthesize these protective proteins. | ||||||
L-Lysine | 56-87-1 | sc-207804 sc-207804A sc-207804B | 25 g 100 g 1 kg | $93.00 $258.00 $519.00 | ||
L-Lysine may facilitate the post-translational modifications of mitochondrial proteins, such as acetylation. This amino acid's presence could enhance the activity of MRP-S35 by promoting the acetylation of proteins that are part of the mitochondrial ribosome, leading to a more active form of MRP-S35 in protein synthesis within the mitochondria. | ||||||
L-Arginine | 74-79-3 | sc-391657B sc-391657 sc-391657A sc-391657C sc-391657D | 5 g 25 g 100 g 500 g 1 kg | $20.00 $30.00 $60.00 $215.00 $345.00 | 2 | |
L-Arginine is involved in nitric oxide synthesis, which can influence mitochondrial function and biogenesis. By enhancing mitochondrial function, L-Arginine can indirectly activate MRP-S35 by increasing the requirement for mitochondrial protein synthesis, thereby stimulating the role of MRP-S35 in the mitochondrial ribosome. | ||||||
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 | $56.00 $186.00 $296.00 $655.00 $2550.00 $3500.00 $10500.00 | 4 | |
NAD+ is a coenzyme involved in redox reactions and is essential for energy metabolism in mitochondria. Elevated levels of NAD+ can stimulate mitochondrial biogenesis and function, which in turn could activate MRP-S35 by increasing the demand for mitochondrial ribosomal proteins necessary for the synthesis of components of the respiratory chain. | ||||||