CECR2 (424-538) GST tag human recombinant, expressed in E. coli, >=95% (SDS-PAGE)

The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as "readers" of histone acetylation marks regulating the transcription of target promoters. Cat eye syndrome critical region protein 2 (CECR2) is a transcription factor that forms a heterodimeric complex with the ATP-dependent chromatin remodeler SNF2L forming the CECR2-containing-remodeling factor (CERF). The CERF complex plays a critical role in neurulation. More recently, the bromodomain of CECR2 was shown to have strong γ-H2AX inhibition activity suggesting that CECR2 may play a role in DNA damage response.