RelB Lentiviral Activation Particles (h): sc-400371-LAC

Human RELB encodes RelB, an NF-κB family transcription factor that primarily functions in the noncanonical NF-κB pathway through heterodimerization with p52 (NFKB2) to regulate context-specific gene expression programs. RelB activity integrates signals from receptors such as BAFFR, CD40, and lymphotoxin-β receptor, shaping immune cell differentiation, lymphoid organogenesis, dendritic cell maturation, and inflammatory responses. Its transcriptional outputs influence cytokine and chemokine networks, cell survival, and antigen presentation pathways, linking RELB to immune dysregulation and inflammation-associated disease biology. Altered RELB signaling has also been studied in oncogenic and microenvironmental programs where NF-κB pathway remodeling contributes to proliferation, stress responses, and immune evasion phenotypes.

RelB 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 RELB upregulation across a broader range of human cell types.

RelB 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 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.