Date published: 2026-7-14

1-800-457-3801

SCBT Portrait Logo
Seach Input

ST8Sia III Lentiviral Activation Particles (h): sc-407120-LAC

0.0(0)
Write a reviewAsk a question

Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • ST8Sia III 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
  • ST8Sia III 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 ST8Sia III Lentiviral Activation Plasmid (h) and ST8Sia III Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ST8SIA3 promoter. One or both designs may be available
    Gene Editing Promo Banner

    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    ST8Sia III Lentiviral Activation Particles (h)

    sc-407120-LAC
    200 µl
    $455.00

    ST8SIA3 encodes the sialyltransferase ST8Sia III, a Golgi-resident enzyme that catalyzes α2,8-linked sialylation of glycoproteins and glycolipids, shaping cell-surface glycan composition and recognition. By regulating polysialylation and related sialylated determinants, ST8Sia III influences cell–cell and cell–matrix interactions, receptor organization, and trafficking within secretory and endocytic pathways. Altered sialylation patterns are associated with changes in adhesion, migration, and immune recognition, making ST8SIA3 relevant to studies of neurodevelopmental processes and tumor-associated glycosylation phenotypes. Functional interrogation of ST8SIA3 can clarify how α2,8-sialylation modulates signaling networks and membrane glycoprotein biology in human cells.

    ST8Sia III 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 ST8SIA3 upregulation across a broader range of human cell types.

    ST8Sia III 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 ST8SIA3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ST8Sia III expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ST8SIA3 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.