Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
IL-27 Lentiviral Activation Particles (m): sc-434233-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- IL-27 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
- IL-27 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 IL-27 Lentiviral Activation Plasmid (m) and IL-27 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Il27 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: IL-27 Antibody (C-8): sc-390482
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
IL-27 Lentiviral Activation Particles (m) | sc-434233-LAC | 200 µl | $455.00 |
Mouse Il27 encodes IL-27, a heterodimeric cytokine in the IL-12 family produced primarily by antigen-presenting cells and acting through the IL-27 receptor complex (WSX-1/IL27RA and gp130). IL-27 activates JAK/STAT signaling, with prominent STAT1 and STAT3 phosphorylation, shaping T helper differentiation, limiting excessive Th17-driven inflammation, and promoting regulatory programs including IL-10 induction in specific contexts. Through these pathways, IL-27 influences innate and adaptive immune crosstalk, antigen presentation, and interferon-associated transcriptional networks. Dysregulated IL-27 signaling has been implicated in models of autoimmunity, chronic inflammation, and infection, making Il27 a useful node for mechanistic immunology studies and pathway mapping.
IL-27 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 Il27 upregulation across a broader range of human cell types.
IL-27 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 Il27 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IL-27 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Il27 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.