Vitamin D Receptor/VDR Lentiviral Activation Particles (h): sc-400171-LAC

VDR encodes the vitamin D receptor, a ligand-activated nuclear receptor that heterodimerizes with RXR and binds vitamin D response elements to regulate transcriptional programs controlling calcium and phosphate homeostasis, epithelial differentiation, and immune modulation. VDR signaling intersects with chromatin remodeling and co-regulator recruitment to shape cell-type-specific gene expression, influencing barrier function, cytokine responses, and metabolic pathways. Dysregulated VDR activity and vitamin D signaling have been associated with altered inflammatory signaling, bone and mineral disorders, and changes in tumor biology in multiple tissues. Human VDR is therefore widely studied in transcriptional regulation, endocrinology, immunology, and epigenetic control of gene networks.

Vitamin D Receptor/VDR 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 VDR upregulation across a broader range of human cell types.

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