Date published: 2026-7-4

1-800-457-3801

SCBT Portrait Logo
Seach Input

ABCA13 Lentiviral Activation Particles (h): sc-407004-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
  • ABCA13 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
  • ABCA13 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 ABCA13 Lentiviral Activation Plasmid (h) and ABCA13 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ABCA13 promoter. One or both designs may be available
    Gene Editing Promo Banner

    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    ABCA13 Lentiviral Activation Particles (h)

    sc-407004-LAC
    200 µl
    $455.00

    ABCA13 encodes an ATP-binding cassette (ABC) transporter of the ABCA subfamily that couples ATP hydrolysis to transmembrane movement of lipids and related hydrophobic substrates. Although its precise substrate specificity remains under active investigation, ABCA13 is implicated in membrane lipid organization, vesicular trafficking, and cellular homeostasis processes that influence epithelial differentiation and barrier biology. Expression and genetic variation in ABCA13 have been associated with altered lipid-handling phenotypes and have been explored in the context of pulmonary and oncogenic biology, including links to tumor behavior and respiratory disease mechanisms. These features make ABCA13 a useful target for studying lipid transport networks, membrane dynamics, and transcriptional programs that modulate cell state.

    ABCA13 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 ABCA13 upregulation across a broader range of human cell types.

    ABCA13 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 ABCA13 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ABCA13 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ABCA13 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.