| Molecular Weight: | 529.34 |
| Formula: | C32H43N5O2 |
| Purity: | ≥ 98% |
| CAS#: | 1415800-43-9 |
| Solubility: | DMSO up to 50 mM |
| Chemical Name: | (2-(phenylamino)-1,4-phenylene)bis((4-(pyrrolidin-1-yl)piperidin-1-yl)methanone) |
| Storage: | Powder: 4oC 1 year. DMSO: 4oC 3 month; -20oC 1 year. |
Biological Activity:
UNC1215 is a highly potent and selective small molecule inhibitor for the methyl-lysine (Kme) reading function of L3MBTL3, a member of the malignant brain tumor (MBT) family of chromatin-interacting transcriptional repressors. UNC1215 binds to L3MBTL3 with a Kd of 120 nM (IC50 ~ 20 nM), competitively displacing mono- or dimethyl-lysine-containing peptides, and is greater than 50-fold more potent toward L3MBTL3 than other members of the MBT family. It also displays >100-fold selectivity over a panel of more than 200 histone methyltransferases, kinases, ion channels and 7-TM receptors. In cells, UNC1215 is nontoxic and directly binds to L3MBTL3 via the Kme-binding pocket of the MBT domains. It 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 was used to reveal a new Kme-dependent interaction of L3MBTL3 with BCLAF1, a protein implicated in DNA damage repair and apoptosis. UNC1215 can serve as a useful chemical tool to interrogate the functions of MBT proteins and probe methyl-lysine reader proteins as a target class.
How to Use:
- In vitro: UNC1215 was used at 1-5 µM final concentration in vitro and in cellular assays.
- In vivo: n/a
Reference:
1. James Li, et al. Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain. (2013) Nat Chem Biol. In press.
Products are for research use only. Not for human use.
