Sm Inhibitors
Chemical inhibitors of Sm proteins disrupt various cellular processes that are essential for the proper function of these proteins in RNA splicing. Amiloride can alter intracellular pH by inhibiting the Na+/H+ exchange process, which is crucial for maintaining the environment necessary for Sm proteins to assemble into spliceosomal snRNPs. Similarly, monensin, as an ionophore, disrupts Na+ gradients, which are essential for maintaining ionic conditions that facilitate the biogenesis and function of Sm protein-containing complexes. Chloroquine raises the pH within acidic vesicles, which can interfere with the intracellular trafficking of snRNPs, essential for the function of Sm proteins in the nucleus. Camptothecin and mitoxantrone, both DNA-damaging agents, can indirectly affect Sm proteins by inhibiting topoisomerase enzymes, thereby leading to transcriptional disturbances that are a prerequisite for the proper assembly of snRNP particles.
Moreover, actinomycin D binds DNA and prevents RNA polymerase from transcribing new RNA, which includes the RNA components necessary for snRNP assembly and, consequently, Sm protein function. Rifampicin, though primarily targeting bacterial RNA polymerase, can also cause a decrease in RNA synthesis in eukaryotic cells, leading to a reduction in the available snRNA for Sm protein binding. Puromycin disrupts protein synthesis, which can reduce the levels of proteins required for snRNP assembly, including Sm proteins. Triptolide's inhibition of transcription can lead to diminished snRNA levels, affecting Sm protein function in snRNPs. Leptomycin B targets the export of RNA/protein complexes from the nucleus, potentially disrupting the Sm protein recycling process. Brefeldin A disrupts the Golgi apparatus, which can indirectly affect Sm proteins by altering the trafficking and modification pathways necessary for their function. Lastly, oxaliplatin forms DNA adducts that can affect transcription, indirectly influencing Sm protein function by impacting the RNA components of snRNPs.
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Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Amiloride | 2609-46-3 | sc-337527 | 1 g | $296.00 | 7 | |
Amiloride inhibits the Na+/H+ exchange process, which is crucial for regulating intracellular pH. Sm proteins are involved in spliceosomal snRNP assembly, a process sensitive to pH changes. Inhibition of Na+/H+ exchange can lead to altered intracellular pH, potentially disrupting snRNP assembly and function. | ||||||
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $155.00 $525.00 | ||
Monensin is an ionophore that disrupts Na+ gradients across membranes, interfering with cellular ion homeostasis. Sm proteins rely on proper ionic conditions for snRNP biogenesis and function, so disruption of Na+ gradients can inhibit the proper assembly or function of these complexes. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $69.00 | 2 | |
Chloroquine raises the pH of acidic vesicles, interfering with vesicle-mediated intracellular trafficking. The trafficking of snRNPs to the nucleus is essential for Sm protein function in RNA splicing, and disruption of this process can inhibit their function. | ||||||
Camptothecin | 7689-03-4 | sc-200871 sc-200871A sc-200871B | 50 mg 250 mg 100 mg | $58.00 $186.00 $94.00 | 21 | |
Camptothecin inhibits topoisomerase I, leading to DNA damage and affecting transcription. While not directly inhibiting Sm proteins, DNA damage can lead to disruptions in RNA processing and splicing, indirectly inhibiting Sm protein function in spliceosomal complexes. | ||||||
Actinomycin D | 50-76-0 | sc-200906 sc-200906A sc-200906B sc-200906C sc-200906D | 5 mg 25 mg 100 mg 1 g 10 g | $74.00 $243.00 $731.00 $2572.00 $21848.00 | 53 | |
Actinomycin D binds to DNA and inhibits RNA polymerase, halting transcription. By preventing the production of new RNA transcripts, the assembly of snRNPs, which require RNA, is indirectly inhibited, thereby inhibiting Sm protein function. | ||||||
Rifampicin | 13292-46-1 | sc-200910 sc-200910A sc-200910B sc-200910C | 1 g 5 g 100 g 250 g | $97.00 $328.00 $676.00 $1467.00 | 6 | |
Rifampicin inhibits bacterial RNA polymerase, and while it is less effective on eukaryotic cells, it can still cause perturbations in RNA synthesis. Reduced RNA levels can lead to a shortage of snRNA for Sm protein binding, indirectly inhibiting Sm protein function. | ||||||
Puromycin | 53-79-2 | sc-205821 sc-205821A | 10 mg 25 mg | $166.00 $322.00 | 436 | |
Puromycin causes premature termination of protein synthesis. By disrupting overall protein synthesis, the concentration of proteins necessary for snRNP assembly, including Sm proteins, can be reduced, indirectly inhibiting their function. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $90.00 $204.00 | 13 | |
Triptolide has been shown to inhibit the transcription of various RNA species. This broad action can lead to decreased snRNA levels, indirectly affecting the availability for Sm protein binding and function in snRNPs. | ||||||
Leptomycin B | 87081-35-4 | sc-358688 sc-358688A sc-358688B | 50 µg 500 µg 2.5 mg | $107.00 $416.00 $1248.00 | 35 | |
Leptomycin B inhibits the nuclear export signal (NES) receptor, which is involved in the export of RNA/protein complexes. By inhibiting this pathway, snRNPs, which include Sm proteins, may be prevented from properly exiting the nucleus, disrupting their recycling and function. | ||||||
Mitoxantrone | 65271-80-9 | sc-207888 | 100 mg | $285.00 | 8 | |
Mitoxantrone intercalates into DNA and inhibits topoisomerase II, leading to DNA damage and affecting transcription processes. This can indirectly affect RNA splicing and thus inhibit Sm protein function by disrupting the RNA components of snRNPs. | ||||||