IRF-7 Lentiviral Activation Particles (h): sc-400450-LAC

IRF7 encodes interferon regulatory factor 7 (IRF-7), a master transcriptional regulator of type I interferon responses downstream of pattern-recognition receptors such as TLR7/9, RIG-I-like receptors, and cGAS–STING signaling. Upon activation, IRF-7 undergoes phosphorylation-dependent dimerization and nuclear translocation to induce IFNA/IFNB and interferon-stimulated gene programs that shape antiviral innate immunity. IRF-7 activity integrates with NF-κB and MAPK pathways to coordinate inflammatory transcriptional networks and innate-adaptive immune crosstalk. Dysregulated IRF7 signaling has been linked to altered antiviral defense, chronic inflammation, and autoimmune phenotypes including systemic lupus erythematosus–associated interferon signatures.

IRF-7 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 IRF7 upregulation across a broader range of human cell types.

IRF-7 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 IRF7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IRF-7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IRF7 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.