Date published: 2026-7-9

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WDR5 Lentiviral Activation Particles (m2): sc-431247-LAC-2

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Datasheets
  • Target species: mouse
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • WDR5 Lentiviral Activation Particles (m2) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
  • WDR5 Lentiviral Activation Particles (m2) 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 WDR5 Lentiviral Activation Plasmid (m2) and WDR5 Lentiviral Activation Plasmid (m22) target distinct regulatory regions of the Wdr5 promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: WDR5 Antibody (G-9): sc-393080
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    WDR5 Lentiviral Activation Particles (m2)

    sc-431247-LAC-2
    200 µl
    $455.00

    Mouse Wdr5 encodes WDR5, a conserved WD40 repeat scaffold protein that is a core component of SET/MLL family histone H3K4 methyltransferase complexes and coordinates chromatin-associated assembly factors to regulate transcriptional programs. WDR5 supports epigenetic control of gene expression through promoter and enhancer regulation, influencing cell cycle progression, lineage specification, and developmental patterning, and it interfaces with broader chromatin remodeling and RNA processing networks. Dysregulated WDR5-dependent chromatin states are linked to altered differentiation and proliferative phenotypes observed in cancer and other epigenetically driven disorders, making Wdr5 a valuable target for mechanistic studies of transcriptional regulation. Gene editing of Wdr5 in mouse models enables functional dissection of H3K4 methylation pathways, mapping of protein–protein interactions within COMPASS/MLL complexes, and investigation of context-specific effects on stem cell biology and tissue homeostasis.

    WDR5 Lentiviral Activation Particles (m2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Wdr5 upregulation across a broader range of human cell types.

    WDR5 Lentiviral Activation Particles (m2) 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 Wdr5 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous WDR5 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Wdr5 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.