1454920-20-7

1454920-20-7 structure

Name: MI-2-2
Chemical Name: 4-[4-(5,5-Dimethyl-4,5-dihydro-1,3-thiazol-2-yl)-1-piperazinyl]-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine
CAS Number: 1454920-20-7
Molecular Formula: C₁₇H₂₀F₃N₅S₂
Molecular Weight: 415.499
Catalog: Signaling Pathways Epigenetics Epigenetic Reader Domain
Create Date: 2018-06-13 18:18:30
Modify Date: 2024-01-02 17:04:38
MI-2-2 is a potent menin-MLL inhibitor. MI-2-2 binds to menin with low nanomolar affinity (Kd=22nM) and very effectively disrupts the bivalent protein-protein interaction between menin and MLL. MI-2-2 has specific and very pronounced activity in MLL leukemia cells, including inhibition of cell proliferation, down-regulation of Hoxa9 expression, and differentiation[1].

Name	4-[4-(5,5-Dimethyl-4,5-dihydro-1,3-thiazol-2-yl)-1-piperazinyl]-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine
Synonyms	Thieno[2,3-d]pyrimidine, 4-[4-(4,5-dihydro-5,5-dimethyl-2-thiazolyl)-1-piperazinyl]-6-(2,2,2-trifluoroethyl)- 4-[4-(5,5-Dimethyl-4,5-Dihydro-1,3-Thiazol-2-Yl)piperazin-1-Yl]-6-(2,2,2-Trifluoroethyl)thieno[2,3-D]pyrimidine 4-[4-(5,5-Dimethyl-4,5-dihydro-1,3-thiazol-2-yl)-1-piperazinyl]-6-(2,2,2-trifluoroethyl)thieno[2,3-d]pyrimidine MFCD29044864

Description	MI-2-2 is a potent menin-MLL inhibitor. MI-2-2 binds to menin with low nanomolar affinity (Kd=22nM) and very effectively disrupts the bivalent protein-protein interaction between menin and MLL. MI-2-2 has specific and very pronounced activity in MLL leukemia cells, including inhibition of cell proliferation, down-regulation of Hoxa9 expression, and differentiation[1].
Related Catalog	Research Areas >> Cancer Signaling Pathways >> Epigenetics >> Epigenetic Reader Domain
In Vitro	MI-2-2 is capable of inhibiting both the interaction of menin with MBM1 (IC50= 46 nM) and with the bivalent fragment of MLL that comprises both MBM1 and MBM2 (IC50=520 nM). MI-2-2 exhibits very pronounced activities at low micromolar concentrations in BMCs transformed with MLL-AF9 and in MV4;11, a human leukemia cell line harboring the MLL-AF4 translocation[1].
References	[1]. Shi A, et al. Structural insights into inhibition of the bivalent menin-MLL interaction by small molecules in leukemia. Blood. 2012;120(23):4461-4469.