RBMXL2 Lentiviral Activation Particles (h): sc-409899-LAC

RBMXL2 (RNA binding motif protein, X-linked-like 2) is a germ cell–enriched RNA-binding protein implicated in post-transcriptional gene regulation, including alternative splicing and mRNA processing. As a member of the RBM family, RBMXL2 is associated with spliceosomal and ribonucleoprotein (RNP) assembly processes that shape cell-type–specific transcript isoforms. Dysregulation of RNA splicing and RNA-binding protein networks is broadly relevant to genome stability, differentiation programs, and stress-responsive transcriptional outputs, providing a framework to examine how RBMXL2-dependent RNA processing contributes to cellular phenotypes. Because RBMXL2 expression is normally restricted and tightly regulated, it can serve as a useful node for studying tissue-specific splicing control and its connections to disease-associated transcriptome alterations.

RBMXL2 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 RBMXL2 upregulation across a broader range of human cell types.

RBMXL2 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 RBMXL2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous RBMXL2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native RBMXL2 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.