Date published: 2026-8-29

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SV2A Lentiviral Activation Particles (m): sc-425665-LAC

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Datasheets
  • Target species: mouse
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • SV2A Lentiviral Activation Particles (m) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
  • SV2A Lentiviral Activation Particles (m) 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 SV2A Lentiviral Activation Plasmid (m) and SV2A Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Sv2a promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: SV2A Antibody (E-8): sc-376234
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    SV2A Lentiviral Activation Particles (m)

    sc-425665-LAC
    200 µl
    $455.00

    Sv2a encodes synaptic vesicle glycoprotein 2A (SV2A), an abundant membrane protein of secretory vesicles that supports Ca2+-dependent neurotransmitter release and presynaptic vesicle cycling. SV2A influences vesicle priming and exocytosis by regulating vesicle protein trafficking and interacting with components of the release machinery, thereby shaping synaptic transmission and network excitability. In the mouse nervous system, SV2A expression is often used as a proxy for synaptic density and maturation, and it is implicated in activity-dependent synaptic remodeling. Altered SV2A levels or function has been associated with neurophysiological dysfunction and seizure-related phenotypes, making Sv2a a useful target for mechanistic studies in neuronal signaling and neurodevelopment.

    SV2A Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Sv2a upregulation across a broader range of human cell types.

    SV2A Lentiviral Activation Particles (m) 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 Sv2a transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SV2A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Sv2a 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.