Date published: 2026-7-26

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FAM20A Lentiviral Activation Particles (m): sc-431579-LAC

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Datasheets
  • Target species: mouse
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • FAM20A 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
  • FAM20A 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 FAM20A Lentiviral Activation Plasmid (m) and FAM20A Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Fam20a promoter. One or both designs may be available
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    FAM20A Lentiviral Activation Particles (m)

    sc-431579-LAC
    200 µl
    $455.00

    Fam20a encodes FAM20A, a secreted pathway protein that functions as a pseudokinase and regulatory partner of the Golgi casein kinase FAM20C, supporting phosphorylation of extracellular matrix and secreted proteins. In mouse tissues, FAM20A contributes to post-translational processing and maturation of mineralized matrix components, linking Golgi/secretory trafficking to extracellular signaling and matrix organization. Disruption of FAM20A–FAM20C-dependent phosphorylation can alter biomineralization and epithelial–mesenchymal interactions, making Fam20a relevant to studies of enamel formation, tissue mineral homeostasis, and secretory pathway biology. Genetic and functional perturbation of Fam20a is therefore used to interrogate extracellular phosphoproteome regulation and matrix-driven developmental phenotypes.

    FAM20A 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 Fam20a upregulation across a broader range of human cell types.

    FAM20A 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 Fam20a transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous FAM20A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Fam20a 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.