ML241 | p97 AAA ATPase inhibitor
NMR (Conforms)
Available Options
| Size: | Price | Quantity | |
|---|---|---|---|
| 5mg | $90.00 | ||
| 25 mg | $360.00 |
ML241 (1346528-06-0) is a potent and selective p97 AAA ATPase inhibitor, IC50=100 nM. Inhibits degradation of a p97-dependent but not p97-independent proteasome substrate in a dual-reporter cell line.1 It impairs the endoplasmic reticulum-associated degradation (ERAD) pathway.1 ML241 and related inhibitors (DBeQ for example) have differential responses to p97 mutants as well as the presence of cofactors suggesting the possibility of context-dependent p97 inhibitors.2,3
References/Citations:
1) Chou et al. (2013), Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase; Chem. Med. Chem., 8 297
2) Chou et al. (2014) Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrate interaction between D1 and D2 ATPase domains; J. Mol. Biol. 426 2886
3) Fang et al. (2015) Evaluating p97 inhibitor analogues for their domain selectivity and potency against the p97-p47 complex; Chem. Med. Chem. 10 52
NMR (Conforms)
Safety Data Sheet:
Product Data Sheet:
Materials provided by Focus Biomolecules are for laboratory research use only and are not intended for human or veterinary applications. Please note that we do not sell to individuals and that all orders placed by non-research organizations will incur a $20 restocking/refund fee
ML241 (1346528-06-0) is a potent and selective p97 AAA ATPase inhibitor, IC50=100 nM. Inhibits degradation of a p97-dependent but not p97-independent proteasome substrate in a dual-reporter cell line.1 It impairs the endoplasmic reticulum-associated degradation (ERAD) pathway.1 ML241 and related inhibitors (DBeQ for example) have differential responses to p97 mutants as well as the presence of cofactors suggesting the possibility of context-dependent p97 inhibitors.2,3
References/Citations:
1) Chou et al. (2013), Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase; Chem. Med. Chem., 8 297
2) Chou et al. (2014) Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrate interaction between D1 and D2 ATPase domains; J. Mol. Biol. 426 2886
3) Fang et al. (2015) Evaluating p97 inhibitor analogues for their domain selectivity and potency against the p97-p47 complex; Chem. Med. Chem. 10 52
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