Anti-CREBBP antibody [EPR24022-28] - BSA and Azide free (Capture)

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

CREBBP also known as CREB Binding Protein or CBP is a multifunctional protein with a molecular weight of approximately 265 kDa. This protein serves as a transcriptional coactivator and possesses intrinsic histone acetyltransferase (HAT) activity. CREBBP is ubiquitously expressed making it present in various tissues throughout the body. Its interaction with different transcription factors facilitates transcriptional activation by remodeling chromatin structure.

Biological function summary

CREBBP plays a pivotal role in regulating gene expression by serving as a coactivator that bridges transcription factors with the basal transcription machinery. CREBBP as part of large multiprotein complexes acetylates histones as well as non-histone proteins influencing chromatin accessibility and transcriptional efficiency. Its HAT activity contributes to the regulation of cell cycle differentiation and DNA repair.

Pathways

CREBBP integrates into both the p53 and Hedgehog signaling pathways modulating various cellular responses. In the p53 pathway CREBBP interacts with the tumor suppressor protein p53 enhancing p53’s ability to initiate expression of genes involved in cell cycle arrest and apoptosis. In the Hedgehog pathway CREBBP regulates transcription factors such as Gli proteins. The interplay between CREBBP and these pathways underlines its importance in maintaining cellular homeostasis and preventing oncogenesis.

Associated diseases and disorders

Mutations or dysregulation of CREBBP are associated with Rubinstein-Taybi syndrome and various cancers including acute myeloid leukemia. In Rubinstein-Taybi syndrome CREBBP mutations impair cognitive development and skeletal malformations. In cancer particularly acute myeloid leukemia alterations in CREBBP disrupt normal cell growth regulation and lead to tumorigenesis. The protein's interaction with factors like p300 another histone acetyltransferase further emphasizes its critical involvement in these pathological conditions.