Chemical inhibitors of IGHMBP2 can exert their inhibitory effects through various cellular mechanisms that are essential for the protein's activity. Alsterpaullone, Olomoucine, Roscovitine, and Paullone share a common mechanism of action as they are all inhibitors of cyclin-dependent kinases (CDKs). CDKs are integral to cell cycle progression and DNA repair, processes in which IGHMBP2 plays a crucial role due to its involvement in DNA unwinding and repair during transcription. By inhibiting CDKs, these chemicals can hinder the cell cycle and DNA repair systems, leading to a functional inhibition of IGHMBP2. Similarly, DRB, a known inhibitor of cellular RNA polymerases, can indirectly inhibit the transcription process where IGHMBP2 operates, thereby leading to its functional inhibition. Aphidicolin, which inhibits DNA polymerases α and δ, can stall the replication fork-a site of action for the IGHMBP2 helicase-thus impeding the protein's ability to facilitate DNA replication.
In addition to the aforementioned CDK inhibitors, Harmine targets dual-specificity tyrosine phosphorylation-regulated kinase (DYRK1A). The inhibition of phosphorylation processes can disrupt the assembly or function of protein complexes involved in DNA unwinding, affecting the helicase activity of IGHMBP2. By a different approach, 5-Iodotubercidin inhibits adenosine kinases, potentially reducing the availability of ATP and consequently the ATPase activity of IGHMBP2, which is vital for its helicase function. Indirubin-3'-monoxime, another CDK and GSK-3β inhibitor, can disrupt cellular processes necessary for IGHMBP2's function, such as DNA replication and repair. Additionally, Camptothecin and Etoposide, which inhibit topoisomerase I and II respectively, induce DNA damage and strand breaks that can affect DNA replication where IGHMBP2 is essential. Finally, Actinomycin D binds to DNA and inhibits the action of RNA polymerase during transcription, which can indirectly inhibit IGHMBP2 by preventing the transcriptional processes where its helicase activity is crucial.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Alsterpaullone | 237430-03-4 | sc-202453 sc-202453A | 1 mg 5 mg | $68.00 $312.00 | 2 | |
Alsterpaullone is a known inhibitor of cyclin-dependent kinases (CDKs). CDKs are essential for the cell cycle progression and DNA repair mechanisms. Since IGHMBP2 is involved in DNA unwinding and repair during transcription, inhibition of CDKs by Alsterpaullone can lead to reduced activity of IGHMBP2 due to impaired DNA repair and replication machinery. | ||||||
Olomoucine | 101622-51-9 | sc-3509 sc-3509A | 5 mg 25 mg | $72.00 $274.00 | 12 | |
Olomoucine is another CDK inhibitor which would act similarly to Alsterpaullone. By inhibiting the CDKs, Olomoucine would disrupt the cell cycle and DNA repair processes, thus potentially reducing the functional activity of IGHMBP2 which requires a properly functioning DNA replication and repair system. | ||||||
Roscovitine | 186692-46-6 | sc-24002 sc-24002A | 1 mg 5 mg | $94.00 $265.00 | 42 | |
Roscovitine selectively inhibits CDKs, which are key regulators of cell cycle and transcription. By inhibiting these kinases, Roscovitine can hinder the proper functioning of DNA replication and repair systems that IGHMBP2 is a part of, leading to its functional inhibition. | ||||||
Harmine | 442-51-3 | sc-202644 sc-202644A sc-202644B sc-202644C sc-202644D sc-202644E sc-202644F | 250 mg 500 mg 1 g 10 g 50 g 100 g 500 g | $53.00 $104.00 $126.00 $551.00 $1467.00 $2611.00 $11455.00 | 2 | |
Harmine is a potent inhibitor of dual-specificity tyrosine phosphorylation-regulated kinase (DYRK1A). Since IGHMBP2 has helicase activity, disruption of phosphorylation processes by Harmine could result in improper assembly or function of the protein complexes involved in DNA unwinding where IGHMBP2 operates. | ||||||
Indirubin-3′-monoxime | 160807-49-8 | sc-202660 sc-202660A sc-202660B | 1 mg 5 mg 50 mg | $79.00 $321.00 $671.00 | 1 | |
This chemical is a known inhibitor of CDKs and glycogen synthase kinase 3 beta (GSK-3β). By inhibiting these kinases, Indirubin-3'-monoxime can disturb cellular processes that are necessary for IGHMBP2 function, such as DNA replication and repair. | ||||||
5-Iodotubercidin | 24386-93-4 | sc-3531 sc-3531A | 1 mg 5 mg | $153.00 $464.00 | 20 | |
This adenosine analog inhibits adenosine kinases. Since IGHMBP2 is an ATP-dependent helicase, inhibition of adenosine kinases by 5-Iodotubercidin can reduce the availability of ATP, thereby potentially inhibiting the ATPase activity of IGHMBP2. | ||||||
DRB | 53-85-0 | sc-200581 sc-200581A sc-200581B sc-200581C | 10 mg 50 mg 100 mg 250 mg | $43.00 $189.00 $316.00 $663.00 | 6 | |
DRB is an adenosine analog that inhibits cellular RNA polymerases. Although not a direct inhibitor of IGHMBP2, by inhibiting RNA polymerases, DRB could indirectly inhibit the transcription process where IGHMBP2 is involved as a helicase, leading to its functional inhibition. | ||||||
Aphidicolin | 38966-21-1 | sc-201535 sc-201535A sc-201535B | 1 mg 5 mg 25 mg | $84.00 $306.00 $1104.00 | 30 | |
Aphidicolin is a tetracyclic diterpene antibiotic that selectively inhibits DNA polymerase α and δ. As IGHMBP2 is involved in DNA unwinding for replication, inhibition of DNA polymerases can indirectly inhibit the function of IGHMBP2 by stalling the replication fork where IGHMBP2 acts. | ||||||
Camptothecin | 7689-03-4 | sc-200871 sc-200871A sc-200871B | 50 mg 250 mg 100 mg | $58.00 $186.00 $94.00 | 21 | |
Camptothecin is a topoisomerase I inhibitor. By stabilizing the transient break which topoisomerase I creates in the DNA strand, it induces DNA damage and can inhibit DNA replication. This could indirectly inhibit the helicase activity of IGHMBP2, which is necessary for DNA replication and repair. | ||||||
Etoposide (VP-16) | 33419-42-0 | sc-3512B sc-3512 sc-3512A | 10 mg 100 mg 500 mg | $51.00 $231.00 $523.00 | 63 | |
Etoposide inhibits DNA topoisomerase II, leading to DNA strand breaks. The resulting DNA damage response can indirectly affect the activity of IGHMBP2 by inhibiting the replication process where the IGHMBP2 helicase is necessary. | ||||||