Anti-CHD4 antibody [EPR12229]

Supplementary info

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

Activity summary

CHD4 also known as CDH4 is a protein that functions as part of the nucleosome remodeling and deacetylase (NuRD) complex. CHD4 has a molecular mass of approximately 218 kDa. The protein contains a chromo domain a helicase domain and two PHD-type zinc fingers. It is expressed ubiquitously in human tissues with higher expression levels seen in the spleen and fetal brain. This protein plays an essential role in DNA transcription regulation by modifying chromatin structure.

Biological function summary

CHD4 acts within the NuRD complex to mediate transcriptional repression. This complex combines chromatin remodeling with histone deacetylation to alter chromatin dynamics affecting gene expression. CHD4's involvement in the complex facilitates the static organization of chromatin therefore contributing to transcriptional silencing of specific gene sets. The protein's activity is often in response to environmental and developmental cues playing an integral role in cellular differentiation and proliferation processes.

Pathways

CHD4 connects closely with DNA damage repair and cell cycle regulation pathways. It participates actively in the DNA damage response pathway by facilitating the repair of double-strand breaks working alongside proteins such as ATM and ATR. CHD4 also influences the cell cycle by interacting with cyclins and cyclin-dependent kinases which maintain proper cell cycle progression and check points.

Associated diseases and disorders

CHD4 has been linked to various cancers and neurodevelopmental disorders. Alterations or mutations in CHD4 have associations with certain cancers like colorectal cancer where it affects cellular proliferation and migration. In neurodevelopmental disorders disrupted CHD4 function may lead to chromatin misregulation contributing to intellectual disabilities. CHD4’s interactions with proteins such as p53 in cancer and MeCP2 in neurological conditions highlight its connections in disease mechanisms.