Date published: 2026-7-13

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IL-4Rα Lentiviral Activation Particles (h): sc-418209-LAC

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Datasheets
  • Target species: human
  • 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
  • IL-4Rα 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
  • IL-4Rα 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 IL-4Rα Lentiviral Activation Plasmid (h) and IL-4Rα Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the IL4R promoter. One or both designs may be available
  • Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: IL-4Rα Antibody (H-4): sc-28361
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    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    IL-4Rα Lentiviral Activation Particles (h)

    sc-418209-LAC
    200 µl
    $455.00

    Human IL4R encodes interleukin-4 receptor alpha (IL-4Rα), a shared receptor subunit for IL-4 and IL-13 that initiates type 2 immune signaling. Ligand engagement promotes receptor complex assembly with IL2RG or IL13RA1, activating JAK1/JAK3-STAT6 signaling and coordinating transcriptional programs involved in Th2 differentiation, IgE class switching, alternative macrophage polarization, and epithelial barrier responses. IL-4Rα also interfaces with IRS/PI3K-AKT and MAPK pathways, shaping cell survival and metabolic rewiring in immune and stromal compartments. Dysregulated IL4R activity has been implicated in atopic inflammation, asthma, and other allergic phenotypes, and it is frequently studied in the context of tumor immune microenvironments and fibrotic remodeling.

    IL-4Rα 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 IL4R upregulation across a broader range of human cell types.

    IL-4Rα 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 IL4R transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IL-4Rα expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IL4R 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.