Apelin Lentiviral Activation Particles (h): sc-401548-LAC

Human APLN encodes apelin, a secreted peptide ligand for the APJ receptor (APLNR) that regulates vascular tone, angiogenesis, fluid homeostasis, and metabolic signaling. Apelin–APLNR engagement activates G protein–coupled pathways including PI3K/AKT, ERK/MAPK, and AMPK, influencing endothelial function, smooth muscle contractility, and cellular survival responses. In disease-relevant contexts, altered apelin signaling has been linked to cardiovascular remodeling, pulmonary hypertension, ischemia responses, and metabolic dysfunction, making APLN a useful node for studying cell–cell communication within vascular and adipose microenvironments. Apelin expression is also responsive to hypoxia and inflammatory cues, supporting investigations into stress-adaptive transcriptional programs.

Apelin 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 APLN upregulation across a broader range of human cell types.

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