LOXL2 Lentiviral Activation Particles (h): sc-401021-LAC

LOXL2 (lysyl oxidase-like 2) is a copper-dependent amine oxidase that catalyzes oxidative deamination of lysine residues in collagen and elastin, promoting covalent crosslinking and extracellular matrix remodeling. Through regulation of matrix stiffness and cell–matrix interactions, LOXL2 influences adhesion, migration, epithelial–mesenchymal transition programs, and fibroblast activation, integrating with TGF-β/SMAD signaling and mechanotransduction pathways such as FAK/SRC and YAP/TAZ. Intracellular LOXL2 has also been linked to chromatin-associated functions that modulate transcriptional states relevant to cellular plasticity. Dysregulated LOXL2 expression is associated with pathological fibrosis and tumor microenvironment remodeling, making it a useful node for studying ECM-driven signaling and invasive phenotypes in human cell models.

LOXL2 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 LOXL2 upregulation across a broader range of human cell types.

LOXL2 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 LOXL2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous LOXL2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native LOXL2 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.