Bcl-3 Lentiviral Activation Particles (h): sc-400740-LAC

BCL3 encodes Bcl-3, an atypical IκB family member that functions predominantly in the nucleus as a transcriptional co-regulator of NF-κB p50 and p52 homodimers. By modulating κB-dependent gene expression, Bcl-3 influences inflammatory signaling, cell-cycle control, and survival programs, and interfaces with pathways governing cytokine responses and differentiation. Dysregulated BCL3 activity has been associated with altered immune cell function and oncogenic transcriptional states, making it a useful node for studying NF-κB pathway dynamics in human cell models. As a context-dependent regulator, Bcl-3 is frequently investigated for its roles in transcriptional reprogramming, chromatin-associated regulation, and stress-responsive signaling.

Bcl-3 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 BCL3 upregulation across a broader range of human cell types.

Bcl-3 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 BCL3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Bcl-3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native BCL3 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.