EXTL1 Lentiviral Activation Particles (h2): sc-409470-LAC-2

Human EXTL1 encodes exostosin-like glycosyltransferase 1, a Golgi-associated enzyme implicated in the biosynthesis and elongation of heparan sulfate chains on proteoglycans, thereby shaping extracellular matrix composition and cell-surface co-receptor function. Through its role in heparan sulfate assembly, EXTL1 influences key signaling networks such as FGF, WNT, and Hedgehog pathways that depend on glycosaminoglycan-mediated ligand distribution and receptor engagement. Dysregulation of heparan sulfate metabolism, including altered EXTL1 activity, has been linked to perturbations in developmental processes and diseases involving aberrant cell communication and matrix remodeling. EXTL1 gene editing or functional perturbation supports mechanistic studies of glycosylation-dependent signaling, proteoglycan biology, and pathway-specific readouts in human cell models.

EXTL1 Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient EXTL1 upregulation across a broader range of human cell types.

EXTL1 Lentiviral Activation Particles (h2) 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 EXTL1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous EXTL1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native EXTL1 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.