RNF31 Lentiviral Activation Particles (h): sc-412436-LAC

Human RNF31 encodes an E3 ubiquitin ligase that serves as the catalytic core of the linear ubiquitin chain assembly complex (LUBAC), generating Met1-linked ubiquitin chains that shape signal propagation downstream of immune receptors. Through regulation of NF-κB and related inflammatory signaling networks, RNF31 influences cytokine responses, cell survival, and stress-adaptive transcriptional programs. RNF31-dependent linear ubiquitination modulates protein complex stability at receptor signaling platforms and contributes to the balance between pro-survival and cell death pathways. Dysregulated RNF31 activity and LUBAC signaling have been associated with aberrant inflammation and oncogenic signaling contexts, supporting its study in immunity, apoptosis, and cancer biology.

RNF31 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 RNF31 upregulation across a broader range of human cell types.

RNF31 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 RNF31 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous RNF31 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native RNF31 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.