A selective inhibitor of the ATPase p97
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ML-240

Item No. 17373

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
2-(2-amino-1H-benzimidazol-1-yl)-8-methoxy-N-(phenylmethyl)-4-quinazolinamine
CAS Number
1346527-98-7
Molecular Formula
C23H20N6O
Formula Weight
396.4
Purity
≥95%
Formulation (Request formulation change)
A crystalline solid
Solubility(Learn about Variance in Solubility)
DMF: 1 mg/mlDMSO: 1 mg/mlDMSO:PBS(pH 7.2) (1:3): 0.25 mg/ml
λmax
254, 304 nm
SMILES
COC1=C2C(C(NCC3=CC=CC=C3)=NC(N4C(C=CC=C5)=C5N=C4N)=N2)=CC=C1
InChi Code
InChI=1S/C23H20N6O/c1-30-19-13-7-10-16-20(19)27-23(28-21(16)25-14-15-8-3-2-4-9-15)29-18-12-6-5-11-17(18)26-22(29)24/h2-13H,14H2,1H3,(H2,24,26)(H,25,27,28)
InChi Key
NHAMBLRUUJAFOY-UHFFFAOYSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    1 mg

    $54

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    5 mg

    $120

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    10 mg

    $185

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    25 mg

    $328

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    Cayman Chemical
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    Product Description

    ML-240 is an ATP-competitive inhibitor of the D2 domain of the ATPase p97 (IC50 = 0.11 µM; Ki = 0.22 µM).1,2 It disrupts the endoplasmic reticulum-associated degradation (ERAD) and autophagy pathways, preventing the degradation of p97-dependent proteasome substrates (IC50 = 0.9 µM) and causing accumulation of ubiquitin conjugates in nuclear membrane and cytosolic compartments at 5-10 µM.1 ML-240 has also been shown to block proliferation of HCT15 and SW403 colon cancer cell lines (GI50s = 0.76 and 0.5 µM, respectively) and to rapidly mobilize caspase-3 and -7, inducing apoptosis.1

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Chou, T.F., Li, K., Frankowski, K.J., et al. Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase. ChemMedChem 8(2), 297-312 (2013).

    2. Chou, T.F., Bulfer, S.L., Weihl, C.C., et al. Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrate interaction between D1 and D2 ATPase domains. J. Mol. Biol. 426(15), 2886-2899 (2014).