Date published: 2026-8-30

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NFATc1 Lentiviral Activation Particles (m): sc-421863-LAC

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Datasheets
  • Target species: mouse
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • NFATc1 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
  • NFATc1 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 NFATc1 Lentiviral Activation Plasmid (m) and NFATc1 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Nfatc1 promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: NFATc1 Antibody (7A6): sc-7294
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    NFATc1 Lentiviral Activation Particles (m)

    sc-421863-LAC
    200 µl
    $455.00

    Nfatc1 encodes NFATc1, a calcium-regulated transcription factor activated downstream of calcineurin following Ca²⁺ influx. NFATc1 coordinates gene expression programs involved in immune-cell activation and differentiation, integrates signals from T cell receptor and cytokine pathways, and cooperates with AP-1 to control transcriptional outputs. In mouse systems, NFATc1 is also a key regulator of osteoclastogenesis and bone remodeling through RANKL-driven signaling, linking this factor to inflammatory processes and skeletal phenotypes. Dysregulated NFATc1 activity has been implicated in aberrant immune responses and pathological tissue remodeling, making it a valuable node for mechanistic studies of signaling-to-transcription coupling.

    NFATc1 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 Nfatc1 upregulation across a broader range of human cell types.

    NFATc1 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 Nfatc1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous NFATc1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Nfatc1 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.