Date published: 2026-8-27

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ZNF71 Lentiviral Activation Particles (h): sc-410081-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • ZNF71 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
  • ZNF71 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 ZNF71 Lentiviral Activation Plasmid (h) and ZNF71 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ZNF71 promoter. One or both designs may be available
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    ZNF71 Lentiviral Activation Particles (h)

    sc-410081-LAC
    200 µl
    $455.00

    ZNF71 encodes a KRAB-domain zinc finger protein that functions as a sequence-specific transcriptional regulator, typically acting in concert with KAP1/TRIM28-associated chromatin remodeling machinery to shape repressive heterochromatin and fine-tune gene expression programs. As part of the broader C2H2 zinc finger network, ZNF71 is linked to control of cellular differentiation states, epigenetic silencing of repetitive elements, and maintenance of transcriptional homeostasis. Dysregulation of KRAB-ZNF factors is frequently studied in the context of altered transcriptional landscapes observed in cancer and other disorders with epigenetic instability, making ZNF71 a relevant node for investigating transcription factor circuitry. Research on ZNF71 commonly intersects pathways governing chromatin accessibility, promoter/enhancer regulation, and context-dependent gene repression or activation.

    ZNF71 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 ZNF71 upregulation across a broader range of human cell types.

    ZNF71 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 ZNF71 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ZNF71 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ZNF71 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.