ACE2 Lentiviral Activation Particles (h): sc-401131-LAC

Angiotensin-converting enzyme 2 (ACE2) is a zinc-dependent carboxypeptidase that counterbalances the renin–angiotensin system by converting angiotensin II to angiotensin-(1–7), thereby modulating vasoregulatory, inflammatory, and fibrotic signaling. Human ACE2 is expressed on epithelial and endothelial surfaces and influences pathways including MAS receptor signaling, oxidative stress responses, and cytokine-associated programs that shape tissue homeostasis. Dysregulated ACE2 expression or activity has been linked to cardiopulmonary and renal pathophysiology, metabolic inflammation, and remodeling processes. ACE2 is also a key host factor in viral entry biology, making it a central node for studying receptor-mediated internalization and downstream innate immune signaling in relevant cell types.

ACE2 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 ACE2 upregulation across a broader range of human cell types.

ACE2 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 ACE2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ACE2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ACE2 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.