NAcM-OPT | NEDD8 ligation inhibitor
NMR (Conforms)
Available Options
| Size : | Price | Quantity | |
|---|---|---|---|
| 5 mg | $55.00 | ||
| 25 mg | $150.00 |
NAcM-OPT (2089293-61-6) is a potent and selective NEDD8 ligation inhibitor, IC50=80 nM (in vitro).1 It inhibits the N-terminal acetyl-dependent interaction between the E2 conjugating enzyme UBE2M/UBC12 and DCN1, a subunit of a multiprotein E3 ligase for the ubiquitin-like protein NEDD8, an interaction which is essential for assembly of the multiprotein ligation complex.2 NAcM-OPT inhibits NEDD8 ligation in vitro and in cells (IC50=10 μM) and suppresses anchorage-independent growth of HCC95 cells and is highly selective with respect to other N-terminal acetyl protein binding sites.1
References/Citations:
1) Scott et al. (2017), Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase; Nat. Chem. Biol., 13 850
2) Scott et al. (2011), N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex; Science, 334 674
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
NAcM-OPT (2089293-61-6) is a potent and selective NEDD8 ligation inhibitor, IC50=80 nM (in vitro).1 It inhibits the N-terminal acetyl-dependent interaction between the E2 conjugating enzyme UBE2M/UBC12 and DCN1, a subunit of a multiprotein E3 ligase for the ubiquitin-like protein NEDD8, an interaction which is essential for assembly of the multiprotein ligation complex.2 NAcM-OPT inhibits NEDD8 ligation in vitro and in cells (IC50=10 μM) and suppresses anchorage-independent growth of HCC95 cells and is highly selective with respect to other N-terminal acetyl protein binding sites.1
References/Citations:
1) Scott et al. (2017), Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase; Nat. Chem. Biol., 13 850
2) Scott et al. (2011), N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex; Science, 334 674
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