
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
RBM15 Lentiviral Activation Particles (h) | sc-417289-LAC | 200 µl | $455.00 |
RBM15 (RNA binding motif protein 15) is a nuclear RNA-binding factor that regulates post-transcriptional gene expression through control of pre-mRNA splicing, transcript stability, and RNA export. It has been linked to epitranscriptomic regulation via association with m6A writer complexes and influences hematopoietic differentiation programs by modulating lineage-specific RNA processing. RBM15 contributes to transcriptional and RNA maturation networks that shape cell fate decisions, with recurrent relevance to dysregulated hematopoiesis. Altered RBM15 function and RBM15-associated fusions have been studied in the context of leukemogenic signaling and broader defects in RNA metabolism.
RBM15 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 RBM15 upregulation across a broader range of human cell types.
RBM15 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 RBM15 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous RBM15 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native RBM15 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.