PADI2 Lentiviral Activation Particles (h): sc-403349-LAC

PADI2 encodes peptidylarginine deiminase 2 (PAD2), a calcium-dependent enzyme that catalyzes citrullination of protein arginine residues, altering charge, structure, and protein–protein interactions. PAD2 activity influences chromatin organization and transcriptional regulation through histone citrullination, and modulates cytoskeletal and immune signaling proteins that shape cell differentiation and inflammatory responses. Dysregulated PADI2 expression or activity has been linked to aberrant immune activation and epigenetic remodeling observed in autoimmune and inflammatory conditions, and it is also studied for roles in tumor-associated transcriptional programs. As a result, PADI2 is a useful node for interrogating post-translational modification pathways, innate/adaptive immune signaling, and gene regulatory networks in human cells.

PADI2 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 PADI2 upregulation across a broader range of human cell types.

PADI2 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 PADI2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PADI2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PADI2 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.