GULP Lentiviral Activation Particles (h): sc-406041-LAC

GULP1 encodes the adaptor protein GULP, a phosphotyrosine-binding domain–containing factor that couples cell-surface engulfment receptors to intracellular signaling during efferocytosis and phagocytosis. GULP functions downstream of receptors such as LRP1/MEGF10 and integrates with cytoskeletal remodeling and membrane trafficking programs to promote clearance of apoptotic cells and cellular debris. Through these processes, GULP influences inflammatory tone and tissue homeostasis by shaping how myeloid and nonprofessional phagocytes resolve cell death. Dysregulation of engulfment and clearance pathways involving GULP1 has been investigated in contexts including neuroinflammation, neurodegeneration, and cancer biology, where altered debris clearance can affect microenvironmental signaling.

GULP 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 GULP1 upregulation across a broader range of human cell types.

GULP 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 GULP1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous GULP expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native GULP1 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.