MATE1 Lentiviral Activation Particles (h): sc-403332-LAC

Human SLC47A1 encodes the multidrug and toxin extrusion protein 1 (MATE1), an apical membrane H+/organic cation antiporter that mediates pH-dependent efflux of endogenous metabolites and xenobiotic organic cations. MATE1 functions in epithelial transport networks, coordinating with uptake transporters in renal proximal tubule and hepatobiliary pathways to regulate cellular clearance and systemic disposition of cationic compounds. Variation or altered expression of SLC47A1 can shift intracellular exposure to substrates and is studied in the context of renal and hepatic transport physiology, drug–drug interaction mechanisms, and toxicity susceptibility. As a transporter at key barrier tissues, MATE1 is commonly interrogated in models of tubular stress, metabolic perturbation, and inflammatory signaling that influence membrane transporter regulation.

MATE1 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 SLC47A1 upregulation across a broader range of human cell types.

MATE1 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 SLC47A1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous MATE1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SLC47A1 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.