glypican-4 Lentiviral Activation Particles (m2): sc-420640-LAC-2

Mouse Gpc4 encodes glypican-4, a glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan that localizes to the cell surface and extracellular matrix to regulate morphogen and growth factor distribution. Glypican-4 modulates signaling pathways including Wnt/β-catenin, FGF, and BMP by shaping ligand–receptor interactions and establishing gradients that influence proliferation, differentiation, and tissue patterning during development. Altered Gpc4 activity or expression is linked to dysregulated extracellular signaling and has been investigated in contexts such as metabolic homeostasis, adipose biology, and neurodevelopmental processes, making it relevant to studies of complex trait genetics. Gene editing of Gpc4 in mouse models supports mechanistic dissection of heparan sulfate–dependent signaling, cell–cell communication, and extracellular matrix regulation across developmental and disease-associated phenotypes.

glypican-4 Lentiviral Activation Particles (m2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Gpc4 upregulation across a broader range of human cell types.

glypican-4 Lentiviral Activation Particles (m2) 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 Gpc4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous glypican-4 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Gpc4 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.