ABP1 Lentiviral Activation Particles (h): sc-410674-LAC

AOC1 encodes amine oxidase copper-containing 1 (ABP1/DAO), a secreted and membrane-associated enzyme that catalyzes oxidative deamination of primary amines, including histamine and polyamines, generating aldehydes, ammonia, and hydrogen peroxide. Through regulation of biogenic amine turnover and reactive oxygen species production, AOC1 influences inflammatory signaling, epithelial barrier function, and cellular redox homeostasis. ABP1 activity intersects with pathways linked to mucosal immunity, vascular biology, and extracellular matrix remodeling, and altered expression has been reported in contexts involving inflammation, allergy, and tumor microenvironment phenotypes. These features make AOC1 a relevant target for mechanistic studies of histamine metabolism, oxidative stress responses, and cell–cell communication in human model systems.

ABP1 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 AOC1 upregulation across a broader range of human cell types.

ABP1 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 AOC1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ABP1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native AOC1 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.