Id2 Lentiviral Activation Particles (h): sc-400550-LAC

Human ID2 encodes inhibitor of DNA binding 2 (Id2), a helix–loop–helix (HLH) protein that lacks a DNA-binding domain and functions primarily by sequestering E-proteins, thereby restraining lineage-specific transcriptional programs. By modulating bHLH-driven gene networks, Id2 regulates cell-cycle progression, differentiation, and maintenance of progenitor-like states across multiple tissues, integrating signals from pathways such as TGF-β/BMP and Notch. Altered ID2 expression is linked to dysregulated differentiation and proliferation phenotypes observed in diverse cancer and immune contexts, making it a frequently studied node in transcriptional and epigenetic control. Researchers commonly examine ID2 to understand how transcription factor antagonism shapes cell fate decisions, stress responses, and developmental programs.

Id2 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 ID2 upregulation across a broader range of human cell types.

Id2 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 ID2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Id2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ID2 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.