A selective inhibitor of the ATPase p97
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ML-241 (hydrochloride)

Item No. 40400

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
2-(2,3-dihydro-4H-1,4-benzoxazin-4-yl)-5,6,7,8-tetrahydro-N-(phenylmethyl)-4-quinazolinamine, monohydrochloride
CAS Number
2070015-13-1
Molecular Formula
C23H24N4O • HCl
Formula Weight
408.9
Purity
≥98%
Formulation
A solid
Solubility(Learn about Variance in Solubility)
Acetonitrile: Slightly solubleDMSO: SolubleWater: Slightly soluble
SMILES
C1(N2C3=CC=CC=C3OCC2)=NC(NCC4=CC=CC=C4)=C(CCCC5)C5=N1.Cl
InChi Code
InChI=1S/C23H24N4O.ClH/c1-2-8-17(9-3-1)16-24-22-18-10-4-5-11-19(18)25-23(26-22)27-14-15-28-21-13-7-6-12-20(21)27;/h1-3,6-9,12-13H,4-5,10-11,14-16H2,(H,24,25,26);1H
InChi Key
DYHMHNNBOLCULH-UHFFFAOYSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    5 mg

    $54

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    10 mg

    $86

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    25 mg

    $162

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    50 mg

    $270

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    Product Description

    ML-241 is an ATP-competitive inhibitor of the ATPase p97 (IC50 = 0.11 µM) that is selective for the D2 domain of p97.1,2 It disrupts the endoplasmic reticulum-associated degradation (ERAD) pathway, preventing the degradation of p97-dependent proteasome substrates in a reporter assay using HeLa cells (IC50 = 3.5 µM) and inducing the accumulation of ubiquitin conjugates in the nuclear plus membrane and cytosolic compartments of SW403 colon cancer cells when used at concentrations of 5 and 10 µM.1 Unlike the p97 inhibitor ML-240, ML-241 does not induce autophagy or apoptosis in, or inhibit the proliferation of, HCT15 and SW403 cancer cells.

    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).