Histone deacetylase 3 (HDAC 3) knockout mouse embryonic stem cell line

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.

Contributors

Inventor Institute
Shaun Cowley University of Leicester
Cat. #: 158386
Unit size: 1×10^6 cells / vial
Research Fields: Developmental biology
Product description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Histone deacetylase 3 (HDAC3) acts as the catalytic core of the SMRT/NCoR co-repressor complex which regulates chromatin structure and gene expression. It was recently shown that HDAC3 binds, and is regulated in vitro, by the binding of inositol phosphates (IP).
Conditional: Yes
Conditional description: Induction of Cre activity by addition of 4-hydroxy tamoxifen (OHT) to the growth media resulted in complete recombination of each allele and deletion of exon 2 (HDAC1Î?‚”2/Î?‚”2 or HDAC2 Î?‚”2/Î?‚”2) within 24 h
Production details: E14 ES cells, expressing a CreER fusion protein from the ROSA26 locus, were used to generate HDAC3Lox/Lox; CreER cell lines by consecutive rounds of gene targeting.
Format: Frozen
Shipping conditions: Dry ice
References:

ANALYSIS OF THE PHYSIOLOGICAL ROLE OF HISTONE DEACETYLASE 3 (HDAC3) AND ITS REGULATION BY INOSITOL PHOSPHATES

Simandi et al. 2016. Mol Cell. 63(4):647-661. PMID: 27499297.

Images

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Quantitative Western blot showing control (-OHT; left) and 4-OHT inducible degradation of HDAC3 protein (right) upon addition to cell culture media. Cells were cultured for 4 days; ?-tubulin was used to normalise protein loading.

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