RelB Lentiviral Activation Particles (m): sc-422643-LAC

Relb encodes RelB, a member of the NF-κB family that functions primarily in the noncanonical NF-κB pathway through heterodimerization with p52 (NFKB2). RelB regulates transcriptional programs controlling dendritic cell maturation, B cell survival, lymphoid organogenesis, and cytokine-driven inflammatory signaling downstream of receptors such as BAFFR, CD40, LTβR, and RANK. In mouse models, altered RelB activity perturbs immune homeostasis and has been linked to chronic inflammation, autoimmunity, and tumor-associated immune regulation. Because RelB integrates developmental and inflammatory cues, it is widely used to study immune cell differentiation, stromal-immune crosstalk, and context-dependent NF-κB transcriptional networks.

RelB Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Relb upregulation across a broader range of human cell types.

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