Furin Lentiviral Activation Particles (h): sc-400904-LAC

FURIN encodes furin, a calcium-dependent proprotein convertase that cycles through the trans-Golgi network and endosomal compartments to proteolytically activate diverse precursor proteins bearing paired basic motifs. By regulating maturation of growth factors, receptors, adhesion molecules, and proteases, furin shapes secretory and membrane protein homeostasis and influences pathways linked to extracellular matrix remodeling, immune signaling, and cellular differentiation. Dysregulated FURIN activity has been associated with altered proteostasis and aberrant processing of signaling components in contexts such as cancer biology, inflammation, and infectious disease research. As a central node in proprotein processing, FURIN provides a mechanistic entry point for studying how precursor cleavage controls cell-surface composition and downstream signaling outputs.

Furin 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 FURIN upregulation across a broader range of human cell types.

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