Histone Deacetylase 11 (HDAC11) Lentiviral Activation Particles (h): sc-402103-LAC

HDAC11 encodes Histone Deacetylase 11, the sole class IV histone deacetylase, which regulates chromatin accessibility and transcriptional programs through lysine deacylation, including deacetylation and defatty-acylation activities. By shaping epigenetic states, HDAC11 influences immune-cell differentiation and inflammatory signaling, impacting pathways that control cytokine expression, antigen presentation, and metabolic adaptation. Altered HDAC11 expression or activity has been linked to dysregulated immune responses and oncogenic transcriptional states, supporting investigation across immunology, hematologic biology, and tumor epigenetics. These functions make HDAC11 a useful node for probing how epigenetic enzymes coordinate gene expression networks that govern proliferation, differentiation, and stress responses.

Histone Deacetylase 11 (HDAC11) Lentiviral Activation Particles (h) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient HDAC11 upregulation across a broader range of human cell types.

Histone Deacetylase 11 (HDAC11) Lentiviral Activation Particles (h) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the HDAC11 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Histone Deacetylase 11 (HDAC11) expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HDAC11 genomic locus and regulatory architecture.

The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.

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