BAT2 Lentiviral Activation Particles (h): sc-409707-LAC

PRRC2A encodes the human BAT2 protein, a large proline-rich RNA-binding factor implicated in post-transcriptional gene regulation and control of mRNA stability and translation. BAT2 has been associated with stress-responsive RNA granule biology and broader regulation of immune-related transcriptional programs, consistent with its genomic proximity to the MHC class III region. Variation or altered expression of PRRC2A/BAT2 has been reported in studies of inflammatory and autoimmune phenotypes and in cancer-related expression signatures, supporting its relevance to pathways governing immune activation, cell-state transitions, and proliferation. These features make PRRC2A a useful node for investigating how RNA regulatory proteins tune signaling outputs in disease-relevant cellular contexts.

BAT2 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 PRRC2A upregulation across a broader range of human cell types.

BAT2 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 PRRC2A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous BAT2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PRRC2A 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.