IFN-β Lentiviral Activation Particles (h): sc-418564-LAC

Human IFNB1 encodes interferon beta (IFN-β), a type I interferon that initiates innate antiviral signaling and shapes downstream adaptive immune responses. IFN-β engages IFNAR to activate JAK1/TYK2-dependent phosphorylation of STAT1/STAT2, forming ISGF3 with IRF9 to induce interferon-stimulated genes that regulate viral restriction, antigen presentation, and apoptosis. Its transcription is triggered by pattern-recognition receptor pathways such as cGAS–STING, RIG-I/MDA5–MAVS, and TLR3–TRIF, converging on IRF3/IRF7 and NF-κB. Dysregulated IFN-β signaling is implicated in interferonopathies and autoimmune inflammation and is widely studied in the context of viral infection, tumor immune evasion, and innate immune sensing of nucleic acids.

IFN-β 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 IFNB1 upregulation across a broader range of human cell types.

IFN-β 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 IFNB1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IFN-β expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IFNB1 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.