Name | UNC 1215 |
Synonyms | CS-714 UNC1215 UNC 1215 UNC1215 UNC-1215 N-Phenyl-2,5-bis({[4-(pyrrolidin-1-yl)piperidin-1-yl]carbonyl})aniline (2-(phenylaMino)-1,4-phenylene)bis((4-(pyrrolidin-1-yl)piperidin-1-yl)Methanone) 1,1'-[2-(Phenylamino)-1,4-phenylene]bis[1-[4-(1-pyrrolidinyl)-1-piperidinyl]methanone] |
CAS | 1415800-43-9 |
Molecular Formula | C32H43N5O2 |
Molar Mass | 529.72 |
Density | 1.224±0.06 g/cm3(Predicted) |
Boling Point | 712.1±60.0 °C(Predicted) |
Solubility | DMSO: soluble5mg/mL, clear |
Appearance | powder |
Color | white to beige |
pKa | 9.90±0.20(Predicted) |
Storage Condition | 2-8°C |
In vitro study | UNC1215 binds to L3MBTL3 and competitively replaces a peptide containing mono-or dimethyl lysine. This probe is 50-fold more selective than acting on other human MBT family members. UNC1215 was approximately 75-fold more selective for L3MBTL3 than for l3mbtl1. At concentrations as high as 30 μm, UNC1215 had no activity on the tandem Tudor domain of UHRF1, the chromatin domain of CBX7, and the PHD domain of JARID1A. X-ray crystallography revealed a unique 2:2 polymodal interaction between UNC1215 and L3MBTL3. UNC1215 is non-toxic to cells, binding directly to L3MBTL3 via the Kme binding pocket of the MBT domain. UNC1215 increases cell mobility and point mutation of GFP-L3MBTL3 fusion protein, interferes with Kme binding function of GFP-L3MBTL3 phenotype simulation, and affects the localization of UNC1215. UNC1215 was used to reveal a novel Kme-dependent L3MBTL3 interaction with BCLAF1, a protein closely related to DNA damage repair and apoptosis. |
WGK Germany | 3 |
1mg | 5mg | 10mg | |
---|---|---|---|
1 mM | 1.888 ml | 9.439 ml | 18.878 ml |
5 mM | 0.378 ml | 1.888 ml | 3.776 ml |
10 mM | 0.189 ml | 0.944 ml | 1.888 ml |
5 mM | 0.038 ml | 0.189 ml | 0.378 ml |