Histone Deacetylase 6 (HDAC6) Lentiviral Activation Particles (m): sc-420820-LAC

Hdac6 encodes histone deacetylase 6 (HDAC6), a predominantly cytoplasmic deacetylase that regulates acetylation of non-histone substrates including α-tubulin, HSP90, and cortactin, thereby influencing microtubule dynamics, chaperone activity, and actin remodeling. Through these functions, HDAC6 coordinates key processes such as autophagy and aggresome-mediated clearance of misfolded proteins, intracellular trafficking, and stress response signaling. HDAC6 activity intersects with proteostasis pathways involving ubiquitin-dependent quality control and can modulate inflammatory signaling and cell motility programs. Dysregulated HDAC6-associated networks have been linked to models of neurodegeneration, cancer-associated phenotypes, and immune-mediated pathology, supporting its broad utility in mechanistic studies.

Histone Deacetylase 6 (HDAC6) Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Hdac6 upregulation across a broader range of human cell types.

Histone Deacetylase 6 (HDAC6) Lentiviral Activation Particles (m) 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 Hdac6 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Histone Deacetylase 6 (HDAC6) expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Hdac6 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.