CDw75/ST6GAL1 Lentiviral Activation Particles (h): sc-402881-LAC

ST6GAL1 encodes beta-galactoside alpha-2,6-sialyltransferase 1 (CDw75), a Golgi-resident enzyme that catalyzes the addition of α2,6-linked sialic acid to terminal galactose residues on N-glycans of glycoproteins and glycolipids. By shaping cell-surface glycosylation patterns, ST6GAL1 influences protein stability, receptor clustering, and ligand recognition, integrating into processes such as immune cell signaling, adhesion, and trafficking. Altered ST6GAL1 activity is frequently studied in the context of cancer-associated glycan remodeling, immune evasion, and metastasis-related phenotypes, as well as inflammatory signaling and hematologic cell differentiation. Its role in modulating sialylation-dependent pathways makes it a key node for investigating glyco-regulatory mechanisms across diverse cell types.

CDw75/ST6GAL1 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 ST6GAL1 upregulation across a broader range of human cell types.

CDw75/ST6GAL1 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 ST6GAL1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CDw75/ST6GAL1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ST6GAL1 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.