Date published: 2026-7-3

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BRD2 Lentiviral Activation Particles (h): sc-402584-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • BRD2 Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
  • BRD2 Lentiviral Activation Particles (h) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
  • Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
  • gRNAs encoded by BRD2 Lentiviral Activation Plasmid (h) and BRD2 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the BRD2 promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: BRD2 Antibody (G-4): sc-393720
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    BRD2 Lentiviral Activation Particles (h)

    sc-402584-LAC
    200 µl
    $455.00

    BRD2 encodes bromodomain-containing protein 2, a BET family chromatin reader that binds acetylated histones to coordinate transcriptional initiation and elongation. BRD2 helps regulate cell-cycle progression, DNA damage responses, and inflammatory gene programs through interactions with transcriptional complexes and chromatin remodeling machinery. It contributes to epigenetic control of gene expression in pathways linked to proliferation and immune signaling, and altered BRD2 activity has been associated with dysregulated transcriptional states observed in cancer and inflammatory disorders. These properties make BRD2 a relevant target for studying chromatin-dependent transcription, enhancer function, and stimulus-responsive gene regulation in human cells.

    BRD2 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 BRD2 upregulation across a broader range of human cell types.

    BRD2 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 BRD2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous BRD2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native BRD2 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.