SBP-2 Inhibitors
Chemical inhibitors of SBP-2 can act through various mechanisms to hinder its function, which is critical in the synthesis of selenoproteins. Ebselen, for instance, can interfere with the enzyme activities necessary for the correct insertion of selenocysteine, a unique amino acid essential for the activity of SBP-2. By inhibiting thioredoxin reductases and glutathione peroxidases, Ebselen disrupts the selenocysteine incorporation process, undermining the proper folding and function of SBP-2. Similarly, Aurintricarboxylic Acid targets the interaction between SBP-2 and SECIS elements in mRNA, a requisite binding for the synthesis of selenoproteins. This binding is crucial for SBP-2's role in the translation of selenoprotein mRNAs, and its inhibition by Aurintricarboxylic Acid compromises SBP-2's function. Methylene Blue affects SBP-2 by altering the redox balance within the cell, which is essential for the redox-dependent activities of SBP-2. As SBP-2 is sensitive to the redox environment due to its role in incorporating selenocysteine, the redox cycling by Methylene Blue can impair its function.
Ethacrynic Acid and Buthionine Sulfoximine target the glutathione metabolism, which is indirectly associated with the activity of SBP-2. Ethacrynic Acid inhibits glutathione S-transferase, potentially affecting the maturation of selenoproteins, while Buthionine Sulfoximine suppresses glutathione synthesis, which may disrupt the cellular redox state necessary for SBP-2 activity. Heavy metal compounds like Cadmium Chloride and Lead(II) Acetate can inhibit SBP-2 through the displacement of metal ions crucial for its activity or by binding to thiol groups, which are important for the protein's conformation and function. The metal chelator Clioquinol could sequester essential metal ions from SBP-2, thereby inhibiting its function. Thimerosal, containing mercury, binds to thiols and can inhibit thiol-dependent domains within SBP-2, leading to functional disruption. Chloroquine, by intercalating into DNA and RNA, can inhibit the necessary protein-RNA interactions involved in SBP-2's function. Lastly, Menadione's redox-cycling ability can alter the redox environment that SBP-2 depends on, thus serving as an inhibitor by modifying the redox conditions required for the proper function of SBP-2.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Ebselen | 60940-34-3 | sc-200740B sc-200740 sc-200740A | 1 mg 25 mg 100 mg | $32.00 $133.00 $449.00 | 5 | |
Ebselen is a seleno-organic compound that can inhibit various enzyme activities, including those of thioredoxin reductases and glutathione peroxidases. SBP-2 requires a specific selenocysteine insertion sequence (SECIS) to incorporate selenocysteine into its structure. Inhibition of thioredoxin reductases by Ebselen could disrupt the proper folding and function of SBP-2 by perturbing the selenocysteine incorporation process. | ||||||
Aurintricarboxylic Acid | 4431-00-9 | sc-3525 sc-3525A sc-3525B sc-3525C | 100 mg 1 g 5 g 10 g | $20.00 $31.00 $47.00 $92.00 | 13 | |
Aurintricarboxylic Acid is known to inhibit nucleic acid-protein interactions. SBP-2's function relies on its binding to SECIS elements in mRNA. By inhibiting this interaction, Aurintricarboxylic Acid could inhibit the function of SBP-2 in the selenoprotein synthesis pathway. | ||||||
Methylene blue | 61-73-4 | sc-215381B sc-215381 sc-215381A | 25 g 100 g 500 g | $42.00 $102.00 $322.00 | 3 | |
Methylene Blue serves as a redox cycling compound and can interfere with redox-sensitive signaling pathways. Since SBP-2 is involved in the synthesis of selenoproteins which have redox functions, Methylene Blue could disrupt the redox state in cells, potentially inhibiting the function of SBP-2 by altering its redox-dependent activities. | ||||||
Ethacrynic acid | 58-54-8 | sc-257424 sc-257424A | 1 g 5 g | $49.00 $229.00 | 5 | |
Ethacrynic Acid is an inhibitor of glutathione S-transferase. SBP-2 interacts with selenoproteins that may require glutathione for proper folding and activity. Inhibition of glutathione S-transferase by Ethacrynic Acid could lead to an environment that is less conducive for selenoprotein maturation, thereby inhibiting SBP-2 function. | ||||||
8-(4-Amino-1-methylbutylamino)-6-methoxyquinoline | 90-34-6 | sc-483239 | 1 g | $360.00 | 1 | |
Primaquine is an antimalarial drug that can cause oxidative stress within the cell. SBP-2 is sensitive to the redox environment due to its role in selenoprotein synthesis. Oxidative stress induced by Primaquine could impair the function of SBP-2 by disrupting the cellular redox balance. | ||||||
L-Buthionine sulfoximine | 83730-53-4 | sc-200824 sc-200824A sc-200824B sc-200824C | 500 mg 1 g 5 g 10 g | $280.00 $433.00 $1502.00 $2917.00 | 26 | |
Buthionine Sulfoximine inhibits the synthesis of glutathione, an important cellular antioxidant. Since SBP-2 is involved in the incorporation of selenocysteine, which has redox functions, lowering glutathione levels could inhibit SBP-2 function by disrupting the cellular redox state necessary for its activity. | ||||||
Cadmium chloride, anhydrous | 10108-64-2 | sc-252533 sc-252533A sc-252533B | 10 g 50 g 500 g | $55.00 $179.00 $345.00 | 1 | |
Cadmium Chloride is a heavy metal compound that can replace other necessary metal ions in proteins and enzymes, potentially disrupting their function. SBP-2, through its interaction with selenoproteins and metal ions, could be inhibited by Cadmium Chloride through the displacement of metal ions critical for its activity. | ||||||
Lead(II) Acetate | 301-04-2 | sc-507473 | 5 g | $83.00 | ||
Lead(II) Acetate can bind to thiol groups and displace other metal ions in proteins. The function of SBP-2 is contingent on its correct conformation and metal ion coordination. Displacement by Lead(II) Acetate could inhibit the proper function of SBP-2. | ||||||
Clioquinol | 130-26-7 | sc-201066 sc-201066A | 1 g 5 g | $44.00 $113.00 | 2 | |
Clioquinol is a metal chelator that can sequester metal ions necessary for protein and enzyme functions. SBP-2 relies on specific metal ions for its activity in selenoprotein synthesis. Chelation by Clioquinol could inhibit SBP-2 by depriving it of essential metal ions. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine is known to intercalate into DNA and RNA, which could inhibit protein-RNA interactions. SBP-2's function involves binding to SECIS elements in mRNA; such interactions could be inhibited by Chloroquine, thus inhibiting SBP-2 activity. | ||||||