C5 Lentiviral Activation Particles (h): sc-401533-LAC

Complement component 5 (C5) is a central effector of the complement cascade, linking C3 convertase activity to formation of the C5 convertase and subsequent generation of C5a and C5b. Proteolytic cleavage of C5 produces C5a, a potent anaphylatoxin that signals through C5a receptors to regulate leukocyte chemotaxis, cytokine release, and vascular inflammation, and C5b, which initiates assembly of the terminal complement complex (MAC, C5b-9) that can lyse susceptible cells. Through these processes, C5 integrates innate immune recognition with inflammatory amplification, opsonophagocytosis support, and pathogen clearance. Dysregulated C5 activation is implicated in inflammatory and autoimmune pathobiology and complement-driven tissue injury, motivating mechanistic studies in immune and vascular models.

C5 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 C5 upregulation across a broader range of human cell types.

C5 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 C5 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous C5 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native C5 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.