IL-13Rα2 Lentiviral Activation Particles (h2): sc-402525-LAC-2
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- IL-13Rα2 Lentiviral Activation Particles (h2) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- IL-13Rα2 Lentiviral Activation Particles (h2) 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-13Rα2 Lentiviral Activation Plasmid (h2) and IL-13Rα2 Lentiviral Activation Plasmid (h22) target distinct regulatory regions of the IL13RA2 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: IL-13Rα2 Antibody (2K8): sc-134363
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
IL-13Rα2 Lentiviral Activation Particles (h2) | sc-402525-LAC-2 | 200 µl | $455.00 |
Human IL13RA2 encodes interleukin-13 receptor alpha 2 (IL-13Rα2), a high-affinity IL-13–binding receptor that modulates type 2 cytokine signaling and can act as a regulatory decoy influencing IL-13 availability and downstream STAT6-dependent transcriptional programs. IL-13Rα2 expression is linked to processes including epithelial–mesenchymal interactions, extracellular matrix remodeling, and inflammatory responses, with crosstalk to pathways governing cell migration and tissue fibrosis. Dysregulated IL13RA2 is frequently associated with tumor biology and immune microenvironment phenotypes, and has been studied in cancers such as glioblastoma as well as in fibrotic and allergic inflammation contexts. Gene editing of IL13RA2 supports mechanistic studies of IL-13 signaling dynamics, receptor-ligand interactions, and functional genomics screens assessing cytokine-driven phenotypes in relevant human cell models.
IL-13Rα2 Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient IL13RA2 upregulation across a broader range of human cell types.
IL-13Rα2 Lentiviral Activation Particles (h2) 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 IL13RA2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IL-13Rα2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IL13RA2 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.