NRAMP 2 Lentiviral Activation Particles (h): sc-418176-LAC

SLC11A2 encodes NRAMP2 (DMT1), a proton-coupled divalent metal ion transporter that mediates cellular uptake and endosomal export of ferrous iron and other transition metals. NRAMP2 is central to intestinal iron absorption and transferrin-cycle iron release in endosomes, linking it to endocytosis, vesicular acidification, and metal homeostasis pathways that influence mitochondrial metabolism and oxidative stress responses. Dysregulation of SLC11A2 is associated with inherited microcytic anemia with iron overload and contributes to iron-handling phenotypes relevant to neurodegeneration, inflammation, and metabolic stress. As a membrane transporter with context-dependent regulation, NRAMP2 is frequently studied in models of nutrient sensing, redox biology, and host–pathogen interactions where metal availability shapes cellular function.

NRAMP 2 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 SLC11A2 upregulation across a broader range of human cell types.

NRAMP 2 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 SLC11A2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous NRAMP 2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SLC11A2 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.