p53-Binding protein 1 (53BP1) binds to dimethylated lysine 20 on histone 4 (H4K20me2) via tandem tudor domains on a 53BP1 homodimer.
货号:ajcx19046
CAS:N/A
分子式:C14H21BrN2O•C4H4O4
分子量：429.3
溶解度:DMF: 30 mg/ml,DMSO: 30 mg/ml,Ethanol: 1 mg/ml,PBS (pH 7.2): 1 mg/ml
纯度：98%
存储：Store at -20°C
库存：现货

Background:

p53-Binding protein 1 (53BP1) binds to dimethylated lysine 20 on histone 4 (H4K20me2) via tandem tudor domains on a 53BP1 homodimer. This interaction is an important part of the DNA damage response. UNC2170 is a micromolar ligand of 53BP1 that binds to a pocket formed by the tandem tudor domains. It displays at least 17-fold selectivity for 53BP1 over other methyl-lysine binding proteins. UNC2170 functions as a 53BP1 antagonist in cellular lysates and shows cellular activity by suppressing class switch recombination, a process which requires a functional 53BP1 tudor domain.