Angptl2 Lentiviral Activation Particles (m): sc-424003-LAC

Mouse angiopoietin-like 2 (Angptl2) is a secreted glycoprotein that modulates vascular and stromal biology by influencing endothelial cell behavior, extracellular matrix remodeling, and tissue inflammation. It is commonly linked to pro-inflammatory signaling networks, including NF-κB–associated transcriptional programs, and can shape leukocyte recruitment and macrophage activation in damaged or metabolically stressed tissues. Angptl2 expression has been associated with adipose tissue dysfunction, insulin resistance–related inflammatory states, vascular remodeling, and tumor-associated microenvironment changes, making it relevant for studies of chronic inflammation and fibrosis-like processes. As a circulating or local paracrine factor, Angptl2 is frequently examined for its effects on cell–cell communication and cytokine/chemokine signaling in organ-specific injury models.

Angptl2 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Angptl2 upregulation across a broader range of human cell types.

Angptl2 Lentiviral Activation Particles (m) 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 Angptl2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Angptl2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Angptl2 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.