PSM Lentiviral Activation Particles (h): sc-401947-LAC

FOLH1 encodes prostate-specific membrane antigen (PSM), a type II transmembrane zinc metallopeptidase with folate hydrolase and NAALADase activities that regulate extracellular folate processing and glutamatergic signaling. The protein influences nutrient uptake and neurotransmitter metabolism through cleavage of poly-γ-glutamated folates and N-acetylaspartylglutamate, linking it to amino acid availability and synaptic homeostasis. FOLH1 expression is highly enriched in prostate epithelium and is broadly used as a molecular marker in studies of prostate biology, while its enzymatic activity in neural tissues supports investigations of excitatory neurotransmission and neuroinflammatory processes. Dysregulated FOLH1/PSM expression and activity have been associated with prostate cancer biology and with pathways relevant to neurodegeneration and tumor-associated microenvironment remodeling.

PSM 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 FOLH1 upregulation across a broader range of human cell types.

PSM 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 FOLH1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PSM expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native FOLH1 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.