BRD4 Lentiviral Activation Particles (h): sc-400519-LAC

BRD4 (bromodomain-containing protein 4) is a chromatin reader that binds acetylated histones through its bromodomains and helps coordinate transcriptional initiation and elongation via recruitment of P-TEFb and regulation of RNA polymerase II pause release. It is a core component of epigenetic control at enhancers and super-enhancers, integrating signaling inputs into gene expression programs that govern cell cycle progression, inflammation, and lineage-specific differentiation. BRD4-dependent transcriptional networks intersect with pathways such as NF-κB signaling and MYC-driven programs, making BRD4 a central node in studies of transcriptional addiction and dysregulated chromatin states. Altered BRD4 activity and enhancer remodeling are associated with proliferative and inflammatory phenotypes, supporting its use in mechanistic research across cancer biology, immunology, and developmental gene regulation.

BRD4 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 BRD4 upregulation across a broader range of human cell types.

BRD4 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 BRD4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous BRD4 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native BRD4 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.