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    InvivoChem Cat #: V0427
    CAS #: 1415800-43-9Purity ≥98%

    Description: UNC1215 (UNC-1215) is a potent and selective antagonist of L3MBTL3, a member of the MBT (malignant brain tumor) family of methyllysine (Kme) reading domain, with potential antineoplastic activity. It inhibits L3MBTL3 with an IC50 of 40 nM and a Kd of 120 nM.

    References: Nat Chem Biol. 2013 Mar;9(3):184-91.

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    Molecular Weight (MW)529.72
    CAS No.1415800-43-9
    Storage-20℃ for 3 years in powder form
    -80℃ for 2 years in solvent
    Solubility (In vitro)DMSO: 100 mg/mL (188.7 mM)
    Water: <1 mg/mL
    Ethanol: 100 mg/mL (188.7 mM)
    Solubility (In vivo) O=C(C1=CC=C(C(N2CCC(N3CCCC3)CC2)=O)C=C1NC4=CC=CC=C4)N5CCC(N6CCCC6)CC5

    UNC-1215, UNC 1215, UNC1215

    Chemical Name: (2-(phenylamino)-1,4-phenylene)bis((4-(pyrrolidin-1-yl)piperidin-1-yl)methanone)


    InChi Code: InChI=1S/C32H43N5O2/c38-31(36-20-12-27(13-21-36)34-16-4-5-17-34)25-10-11-29(30(24-25)33-26-8-2-1-3-9-26)32(39)37-22-14-28(15-23-37)35-18-6-7-19-35/h1-3,8-11,24,27-28,33H,4-7,12-23H2 

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    In Vitro

    In vitro activity: UNC1215 binds L3MBTL3, competitively displacing mono- or dimethyllysine-containing peptides. This probe is greater than 50-fold selective versus other members of the human MBT family. UNC1215 has about a 75-fold selectivity for L3MBTL3 over L3MBTL1. UNC1215 shows no activity at concentrations up to 30 μM against the tandem Tudor domain of UHRF1, the chromodomain of CBX7 or the PHD domain of JARID1A. X-ray crystallography identifies a unique 2:2 polyvalent mode of interaction between UNC1215 and L3MBTL3. In cells, UNC1215 is nontoxic and directly binds L3MBTL3 via the Kme-binding pocket of the MBT domains. UNC1215 increases the cellular mobility of GFP-L3MBTL3 fusion proteins, and point mutants that disrupt the Kme-binding function of GFP-L3MBTL3 phenocopy the effects of UNC1215 on localization. UNC1215 is used to reveal a new Kme-dependent interaction of L3MBTL3 with BCLAF1, a protein implicated in DNA damage repair and apoptosis.

    Kinase Assay: Compound plates (1 μL at 10 or 30 mM highest concentration) are diluted in 1×assay buffer (20 mM Tris pH 8.0, 25 mM NaCl, 2 mM DTT and 0.05% Tween-20) over 2 steps using a Multimek robotic pipettor and 1 μL is spotted into the wells of 384-well assay Proxiplates. To these plates 9 μL of protein- peptide mix in 1× assay buffer is added by Multidrop and incubated for 30 min at room temperature. At this point 2 μL of streptavidin-conjugate donor and nickel-chelate acceptor beads (45 μg/mL in 1× assay buffer) are added, the plates are allowed to incubate for an additional 30 min in the dark at room temperature. After incubation the plates are read on EnVision mulilabel reader equipped with HTS alpha screen laser. The screens reported are performed up to 10 or 30 μM, and therefore it should be noted that those compounds referred to as inactive are indeed inactive only within the concentration range tested. PHF23 and JARID1A are GST tagged and consequently for these assays GST-acceptor beads are used. It should be noted that any positive binding curves for L3MBTL4 that are generated yielded curves with very shallow slopes, suggesting a nonspecific interaction. The data for the IC50 values is calculated from replicate runs in that the datapoints for each compound concentration are averaged and plotted using 4-parameters curve fitting.

    Cell Assay: CellTiter-Glo luminescent cell viability assay using HEK293T/17 cells.

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    Nat Chem Biol. 2013 Mar;9(3):184-91.

    These protocols are for reference only. InvivoChem does not independently validate these methods.


    UNC1215 is a potent antagonist of L3MBTL3.  2013 Mar;9(3):184-91. 


    X-ray crystal structure of the UNC1215-3MBT complex.  2013 Mar;9(3):184-91. 


    UNC1215 binds a small set of Kme reader proteins with lower affinity than L3MBTL3.  2013 Mar;9(3):184-91.


    UNC1215 potently antagonizes 3MBT localization in cells.  2013 Mar;9(3):184-91. 


    UNC1215 binds and co-localizes with full length L3MBTL3

    (a) UNC1215 conjugated to the cell-permeable merocyanine dye, mero-76, co-localizes with GFP-FLMBT in HEK293 cells (scale bar, 10 μm; green is GFP-FLMBT, red is merocyanine-UNC1215, and blue is Hoechst dye). (b) FLMBT binds to biotin-UNC1215 (5 nmol).  2013 Mar;9(3):184-91.


    Identification of BCLAF1 as a novel L3MBTL3 protein interactor

    (a) In U2OS cells, 3MBT colocalizes with BCLAF1 (top panel; green is GFP-3MBT, red is BCLAF, and blue is DAP1). Upon treatment with UNC1215, the 3MBT and BCLAF1 nuclear foci are noticeably disrupted (bottom panel). (b) Immunoprecipitation experiments in cells transfected with flag-3MBT or flag-FLMBT show that UNC1215 disrupts the interaction between 3MBT and BCLAF1 and also reduces the interaction between FLMBT and BCLAF1.   2013 Mar;9(3):184-91.


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