CREBBP Protein, Human (His)

CREBBP Protein, Human (His) is the recombinant human-derived CREBBP, expressed by E. coli , with N-6*His labeled tag.

CREBBP is an acetyltransferase that acetylates histones (e.g., H3K18ac and H3K27ac), providing specific marks for transcriptional activation. It also acetylates non-histone proteins, including DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53, and FOXO1. CREBBP specifically binds phosphorylated CREB, enhancing its transcriptional activity toward cAMP-responsive genes, and acts as a coactivator for ALX1. It functions as a circadian transcriptional coactivator by enhancing the activity of NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers. During nucleotide excision repair (NER), CREBBP acetylates PCNA, promoting its removal from chromatin and degradation. Additionally, it acetylates POLR1E/PAF53, reducing RNA polymerase I association with the rDNA promoter and coding regions. CREBBP inhibits DDX21 helicase activity via acetylation and prevents histone H2A Gln-105 methylation (H2AQ104me) by acetylating FBL. Beyond protein acetylation, CREBBP utilizes different acyl-CoA substrates (e.g., lactoyl-CoA) to mediate protein lactylation, such as MRE11 lactylation in response to DNA damage, promoting homologous recombination (HR)-mediated DNA double-strand break (DSB) repair. It also serves as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway.

Human

E. coli

N-6*His

Q92793-1 (R1081-G1197)

1387

Partial

Approximately 13-15 kDa,based on SDS-PAGE under reducing conditions.

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.