Date published: 2026-7-14

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cGAS Lentiviral Activation Particles (h): sc-403354-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • cGAS 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
  • cGAS 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 cGAS Lentiviral Activation Plasmid (h) and cGAS Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the MB21D1 promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: cGAS Antibody (D-9): sc-515777
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    cGAS Lentiviral Activation Particles (h)

    sc-403354-LAC
    200 µl
    $455.00

    Human MB21D1 encodes cyclic GMP-AMP synthase (cGAS), a cytosolic DNA sensor that catalyzes synthesis of 2′3′-cGAMP to activate STING (TMEM173) and downstream TBK1–IRF3 and NF-κB signaling. This pathway coordinates type I interferon and inflammatory gene programs in response to microbial DNA, genomic instability, and mislocalized self-DNA from micronuclei or mitochondrial stress. cGAS signaling intersects with DNA damage responses, chromatin regulation, autophagy, and senescence-associated inflammation, shaping innate immune tone across tissues. Dysregulated cGAS–STING activity has been implicated in autoinflammatory phenotypes, cancer immune microenvironment remodeling, and neuroinflammation, supporting its frequent use in mechanistic studies of nucleic acid sensing.

    cGAS 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 MB21D1 upregulation across a broader range of human cell types.

    cGAS 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 MB21D1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous cGAS expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native MB21D1 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.