BPAG1 Lentiviral Activation Particles (h): sc-403388-LAC

DST encodes bullous pemphigoid antigen 1 (BPAG1), a large plakin-family cytolinker that couples intermediate filaments to membrane-associated adhesion complexes and helps maintain cytoskeletal architecture under mechanical stress. Through its multiple isoforms, BPAG1 coordinates actin–microtubule–intermediate filament cross-talk, contributing to hemidesmosome stability, intracellular trafficking, and neuronal cytoskeletal organization. Disruption of BPAG1-linked networks is associated with impaired epidermal integrity and neuromuscular function, making DST a useful entry point for studying adhesion-dependent signaling and cytoskeleton-driven cell resilience. These properties connect DST/BPAG1 biology to pathways governing cell–matrix attachment, mechanotransduction, and stress response in epithelial and neuronal systems.

BPAG1 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 DST upregulation across a broader range of human cell types.

BPAG1 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 DST transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous BPAG1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native DST 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.