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In the intact cell, DNA closely associates with histones and other nuclear proteins to form chromatin. The remodeling of chromatin is believed to be a critical component of transcriptional regulation and a major source of this remodeling is brought about by the acetylation of nucleosomal histones. Acetylation of lysine residues in the amino terminal tail domain of histone results in an allosteric change in the nucleosomal conformation and an increased accessibility to transcription factors by DNA. Conversely, the deacetylation of histones is associated with transcriptional silencing. Several mammalian proteins have been identified as nuclear histone acetylases, including GCN5, PCAF (p300/CBP-associated factor), p300/CBP, HAT1 and the TFIID subunit TAF II p250. Mammalian HDAC8, isolated from human kidney, is a histone deacetylase that shares homology to other HDACs but has different tissue distribution. HDAC8 is localized to the nucleus and plays a role in the development of a broad range of tissues and in the etiology of cancer.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: HD8; Histone deacetylase 8; histone deacetylase-like 1; Protein deacetylase HDAC8; Protein decrotonylase HDAC8
基因别名: CDA07; CDLS5; HD8; HDAC8; HDACL1; MRXS6; RPD3; WTS
UniProt ID: (Human) Q9BY41
Entrez Gene ID: (Human) 55869