Date published: 2026-7-9

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WDR20 Lentiviral Activation Particles (h): sc-418266-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • WDR20 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
  • WDR20 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 WDR20 Lentiviral Activation Plasmid (h) and WDR20 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the WDR20 promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: WDR20 Antibody (38K): sc-100900
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    WDR20 Lentiviral Activation Particles (h)

    sc-418266-LAC
    200 µl
    $455.00

    WDR20 encodes a WD-repeat scaffolding protein that functions as a regulatory cofactor for deubiquitinating enzyme complexes, helping coordinate ubiquitin-dependent control of protein stability and signaling. Through modulation of deubiquitination, WDR20 influences cellular proteostasis and pathway dynamics linked to cell growth, stress responses, and transcriptional programs. Perturbation of ubiquitin signaling networks involving WDR20 has been associated with altered cellular homeostasis and has relevance to disease biology where ubiquitin-mediated regulation is disrupted, including contexts of malignant transformation and neurobiological dysfunction. As such, WDR20 is a useful node for dissecting how deubiquitination tunes pathway output and protein turnover in human cells.

    WDR20 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 WDR20 upregulation across a broader range of human cell types.

    WDR20 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 WDR20 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous WDR20 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native WDR20 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.