Description
Short Description: The peptide corresponding to amino acids 1081-1197 that contains the bromodomain sequences of CREBBP (accession number NM_004380.2) was expressed in E Coli and contains an N-terminal His-tag and C-terminal DYKDDDDK tag with an observed molecular weight of 18.7 kDa. It shows binding specificity for acetylated H2BK85, H3K9/K14, H3K14, H3K36, H3K56, H3S10/K14/K18, H4K12, H4K20 and H4K44, as well as acetylated p53-K382, MyoD-K99 and MyoD-K99/K102. CREB-binding protein (CREBBP) or CBP, is a protein known to play critical roles in embryonic development, growth control, and homeostasis by coupling chromatin remodeling to transcription factor recognition. CREBBP shares regions of very high sequence similarity with protein p300 in its bromodomain, cysteine-histidine-rich regions, and histone acetyltransferase domain. The CREBBP bromodomain recognizes acetylated histone lysine residues and functions as a 'reader' of these epigenetic histone marks to regulate chromatin structure and gene expression by linking associated proteins to the recognized acetylated nucleosomal targets. CREBBP has intrinsic histone acetyltransferase activity and also acts as a scaffold to stabilize additional protein interactions with the transcription complex. CREBBP acetylates histones as well as non-histone proteins, like NCOA3 coactivator. In addition, CREBBP binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. CREBBP also has been shown to act as a coactivator of ALX1 in the presence of p300. Recombinant CREBBP (1081-1197) can be used in binding assays and inhibitor screening