LAR Lentiviral Activation Particles (h): sc-402674-LAC

Protein tyrosine phosphatase receptor type F (PTPRF), also known as LAR, is a receptor-like protein tyrosine phosphatase that modulates phosphorylation-dependent signaling at the plasma membrane and cell–cell or cell–matrix interfaces. LAR influences focal adhesion dynamics, neurite outgrowth, and synaptic organization by regulating pathways downstream of receptor tyrosine kinases and integrin-associated signaling, impacting cytoskeletal remodeling and cellular migration. Through its extracellular adhesion-like domains and intracellular phosphatase activity, PTPRF can tune MAPK/ERK and PI3K/AKT pathway outputs via dephosphorylation of select substrates. Dysregulated PTPRF/LAR signaling has been associated with altered metabolic signaling and neurodevelopmental or neurodegenerative phenotypes, making it relevant for mechanistic studies in insulin signaling, neuronal connectivity, and invasion-related cellular programs.

LAR 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 PTPRF upregulation across a broader range of human cell types.

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