PTP1B Lentiviral Activation Particles (h): sc-400732-LAC

PTPN1 encodes protein tyrosine phosphatase 1B (PTP1B), an endoplasmic reticulum–associated phosphatase that dephosphorylates activated receptor tyrosine kinases and key signaling intermediates. By attenuating insulin receptor and IGF1R signaling, PTP1B modulates PI3K–AKT and MAPK pathway output, shaping cellular metabolism, growth-factor responsiveness, and stress signaling. PTP1B also influences cytokine and JAK/STAT-related signaling through dephosphorylation of selected substrates, linking phosphotyrosine turnover to inflammatory and immune regulatory processes. Dysregulated PTPN1/PTP1B activity has been implicated in metabolic phenotypes, cancer-associated signaling rewiring, and altered immune signaling, making it a widely used node for pathway dissection.

PTP1B 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 PTPN1 upregulation across a broader range of human cell types.

PTP1B 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 PTPN1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PTP1B expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PTPN1 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.