Histone Deacetylase 2 (HDAC2) CRISPR Activation Plasmid (h): sc-400303-ACT

HDAC2 encodes histone deacetylase 2, a class I HDAC that removes acetyl groups from lysine residues on histone tails to promote chromatin compaction and transcriptional repression. As a catalytic component of multiprotein corepressor complexes such as NuRD, Sin3, and CoREST, HDAC2 helps regulate cell-cycle progression, DNA damage responses, differentiation programs, and neuronal plasticity through epigenetic control of gene expression. By coordinating histone and non-histone deacetylation, HDAC2 influences signaling outputs from pathways that converge on chromatin remodeling and transcription factor accessibility. Dysregulated HDAC2 activity or expression has been associated with altered epigenomic states observed in cancer biology, neurodevelopmental and neurodegenerative processes, and inflammatory gene regulation.

Histone Deacetylase 2 (HDAC2) CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous HDAC2 expression without altering the underlying DNA sequence.

Histone Deacetylase 2 (HDAC2) CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the HDAC2 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.

Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the HDAC2 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous Histone Deacetylase 2 (HDAC2) expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native HDAC2 locus and enabling the study of Histone Deacetylase 2 (HDAC2)-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of Histone Deacetylase 2 (HDAC2) pathway restoration in tumor cells with silenced or reduced HDAC2 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.