Date published: 2026-9-10

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utrophin Lentiviral Activation Particles (h): sc-400522-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • utrophin 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
  • utrophin 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 utrophin Lentiviral Activation Plasmid (h) and utrophin Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the UTRN promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: utrophin Antibody (8A4): sc-33700
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    utrophin Lentiviral Activation Particles (h)

    sc-400522-LAC
    200 µl
    $455.00

    utrophin Lentiviral Activation Particles (h2)

    sc-400522-LAC-2
    200 µl
    $455.00

    Human UTRN encodes utrophin, a dystrophin-associated cytoskeletal adaptor that links F-actin to the dystroglycan complex at the sarcolemma, helping organize membrane stability and signal transduction. Utrophin participates in assembly and maintenance of the dystrophin–glycoprotein complex and interfaces with extracellular matrix interactions that influence mechanotransduction and cell polarity. Its expression is developmentally regulated and can be modulated in response to muscle injury and remodeling, making it relevant to studies of myofiber integrity and neuromuscular junction organization. Altered utrophin levels and localization are commonly examined in the context of dystrophinopathies and related muscle degeneration models as a functional paralog within the same structural pathway.

    utrophin 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 UTRN upregulation across a broader range of human cell types.

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