Date published: 2026-8-17

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Laminin γ-2 Lentiviral Activation Particles (h): sc-401068-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • Laminin γ-2 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
  • Laminin γ-2 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 Laminin γ-2 Lentiviral Activation Plasmid (h) and Laminin γ-2 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the LAMC2 promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: Laminin γ-2 Antibody (E-6): sc-28330
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    Laminin γ-2 Lentiviral Activation Particles (h)

    sc-401068-LAC
    200 µl
    $455.00

    LAMC2 encodes the laminin γ2 chain, a key component of laminin-332 in basement membranes that supports epithelial adhesion, polarity, and tissue integrity. Through interactions with integrins such as α3β1 and α6β4, laminin γ2 contributes to focal adhesion signaling, hemidesmosome organization, and downstream pathways including FAK/Src, PI3K–AKT, and MAPK that regulate migration and survival. Proteolytic processing of laminin-332 can generate motility-promoting fragments, linking LAMC2 to dynamic remodeling of the extracellular matrix during wound repair. Dysregulated LAMC2 expression and altered laminin-332 assembly are frequently studied in epithelial barrier defects and tumor-associated invasion programs as biomarkers of basement-membrane disruption.

    Laminin γ-2 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 LAMC2 upregulation across a broader range of human cell types.

    Laminin γ-2 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 LAMC2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Laminin γ-2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native LAMC2 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.