RPAIN inhibitors belong to a class of chemical compounds that modulate the activity of RPA-interacting protein (RPAIN). RPAIN is a critical regulatory protein involved in the DNA damage response, particularly in the control of replication protein A (RPA), a key player in DNA replication, recombination, and repair. RPAIN's function includes mediating the nuclear-cytoplasmic shuttling of RPA and its interaction with other proteins during the DNA repair process. By influencing the localization and activity of RPA, RPAIN plays a pivotal role in maintaining genomic stability. Inhibitors of RPAIN interfere with its ability to bind RPA, thus modulating DNA repair pathways and potentially altering cellular responses to DNA damage. These inhibitors are useful tools for studying the biochemical mechanisms of DNA damage recognition and repair, allowing researchers to probe the molecular intricacies of cellular responses to genotoxic stress.
The mechanism of RPAIN inhibitors typically involves competitive or non-competitive binding to the active or regulatory sites of the protein. This binding alters the conformation or the interaction capacity of RPAIN, thereby impeding its normal function in modulating RPA. Structural analyses of these inhibitors often reveal interactions with specific amino acid residues within RPAIN's functional domains, providing insights into their specificity and efficacy. Beyond their value in elucidating DNA repair pathways, RPAIN inhibitors serve as important molecular probes in biochemical research, enabling deeper investigation into protein-protein interactions, post-translational modifications, and the broader cellular mechanisms governing genomic maintenance. Their study is fundamental in advancing the understanding of DNA repair fidelity and the regulation of replication processes in complex biological systems.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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Pladienolide B | 445493-23-2 | sc-391691 sc-391691B sc-391691A sc-391691C sc-391691D sc-391691E | 0.5 mg 10 mg 20 mg 50 mg 100 mg 5 mg | $290.00 $5572.00 $10815.00 $25000.00 $65000.00 $2781.00 | 63 | |
Inhibits spliceosome function, potentially affecting RNA splicing where RPAIN might be involved. | ||||||
Leptomycin B | 87081-35-4 | sc-358688 sc-358688A sc-358688B | 50 µg 500 µg 2.5 mg | $105.00 $408.00 $1224.00 | 35 | |
Inhibits nuclear export by binding to exportin 1, potentially influencing RPAIN's role in RNA transport. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $88.00 $200.00 | 13 | |
Inhibits RNA polymerase II, potentially reducing the transcription of genes involved in pathways where RPAIN operates. | ||||||
BMH-21 | 896705-16-1 | sc-507460 | 10 mg | $165.00 | ||
A small molecule that binds to RNA polymerase I, potentially altering ribosomal RNA production and impacting RPAIN activity. | ||||||
Silvestrol | 697235-38-4 | sc-507504 | 1 mg | $920.00 | ||
Inhibits eukaryotic initiation factor 4A, potentially affecting the translation of mRNAs that RPAIN is involved with. | ||||||
CX-5461 | 1138549-36-6 | sc-507275 | 5 mg | $240.00 | ||
Inhibits RNA polymerase I, potentially impacting ribosomal RNA synthesis and indirectly affecting RPAIN function. | ||||||
Flavopiridol Hydrochloride | 131740-09-5 | sc-207687 | 10 mg | $311.00 | ||
Inhibits cyclin-dependent kinases, potentially affecting cell cycle-related processes and the function of RPAIN. | ||||||
DRB | 53-85-0 | sc-200581 sc-200581A sc-200581B sc-200581C | 10 mg 50 mg 100 mg 250 mg | $42.00 $185.00 $310.00 $650.00 | 6 | |
Inhibits RNA polymerase II, potentially reducing transcription where RPAIN may be implicated. | ||||||
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 | $73.00 $238.00 $717.00 $2522.00 $21420.00 | 53 | |
Interferes with RNA polymerase, potentially decreasing RNA synthesis involving RPAIN-associated pathways. | ||||||
ICRF-193 | 21416-68-2 | sc-200889 sc-200889A | 1 mg 5 mg | $330.00 $898.00 | 7 | |
Binds to topoisomerase II, potentially affecting DNA topology and transcription where RPAIN is functional. |