
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
IFITM1 Lentiviral Activation Particles (h) | sc-416878-LAC | 200 µl | $455.00 |
IFITM1 (interferon-induced transmembrane protein 1) is an interferon-stimulated gene that encodes a small membrane-associated protein involved in intrinsic antiviral defense. IFITM1 modulates cellular membrane properties and endosomal trafficking to restrict viral entry and fusion, integrating with type I/II interferon signaling and broader innate immune pathways such as JAK–STAT-driven transcriptional programs. Beyond host–pathogen interactions, altered IFITM1 expression has been linked to immune activation states and inflammatory microenvironments, with reported associations to tumor biology and metastatic behavior in multiple cancer contexts. These features make IFITM1 a useful node for studying interferon responsiveness, cell-intrinsic immunity, and membrane-dependent regulation of pathogen uptake.
IFITM1 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 IFITM1 upregulation across a broader range of human cell types.
IFITM1 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 IFITM1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IFITM1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IFITM1 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.