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:
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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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