UNC1215

Research use only, not for human use.

A potent and selective chemical probe for the methyllysine (Kme) reading function of L3MBTL3 with Kd of 120 nM.

A potent and selective chemical probe for the methyllysine (Kme) reading function of L3MBTL3 with Kd of 120 nM; 50-fold more potent toward L3MBTL3 than other members of the MBT family; directly binds to L3MBTL3 via the Kme-binding pocket of the MBT domains.

UNC1215 binds L3MBTL3 with a d of 120 nM, competitively displacing mono- or dimethyllysine-containing peptides, and is greater than 50-fold more potent toward L3MBTL3 than other members of the MBT family while also demonstrating selectivity against more than 200 other reader domains examined. X-ray crystallography identified 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.

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UNC 1215 | UNC-1215

Chromatin/Epigenetic

HMTase

L3MBTL3|L3MBTL3-D274A

Other Indications

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1415800-43-9

529.7161

C32H43N5O2

>98% (HPLC)

DMSO: ≥ 270 mg/mL

O=C(C1=CC=C(C(N2CCC(N3CCCC3)CC2)=O)C=C1NC4=CC=CC=C4)N5CCC(N6CCCC6)CC5

Methanone, 1,1'-[2-(phenylamino)-1,4-phenylene]bis[1-[4-(1-pyrrolidinyl)-1-piperidinyl]-

(-20℃)

With Ice Pack

≥ 2 years