FANCI Lentiviral Activation Particles (h): sc-402229-LAC

Human FANCI encodes a core component of the Fanconi anemia (FA) DNA repair network that safeguards genome integrity during DNA replication. FANCI forms the ID2 complex with FANCD2 and undergoes ATR-dependent phosphorylation and FA core complex–mediated monoubiquitination, enabling recruitment of downstream nucleases and homologous recombination factors to resolve DNA interstrand crosslinks and stalled replication forks. Through its roles in replication fork protection, S-phase checkpoint signaling, and repair coordination, FANCI dysfunction is linked to chromosomal instability and the pathobiology of Fanconi anemia and related cancer predisposition syndromes. As a readout in mechanistic studies, FANCI activity can be monitored via ID2 monoubiquitination, RAD51 focus formation, and sensitivity to crosslinking agents.

FANCI 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 FANCI upregulation across a broader range of human cell types.

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