RBP2 Lentiviral Activation Particles (m): sc-431972-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- RBP2 Lentiviral Activation Particles (m) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- RBP2 Lentiviral Activation Particles (m) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
- Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
- gRNAs encoded by RBP2 Lentiviral Activation Plasmid (m) and RBP2 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Kdm5a promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: RBP2 Antibody (G-12): sc-365993
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
RBP2 Lentiviral Activation Particles (m) | sc-431972-LAC | 200 µl | $455.00 |
Kdm5a encodes RBP2 (also known as JARID1A), a Fe(II)/2-oxoglutarate–dependent histone demethylase that primarily removes H3K4me3/2 marks to modulate transcriptional initiation and chromatin accessibility. In mouse cells, RBP2 integrates into epigenetic regulatory networks controlling cell-cycle progression, lineage specification, and differentiation programs, and it can coordinate with retinoblastoma (RB) pathway–associated transcriptional complexes. By shaping promoter and enhancer states, Kdm5a influences processes such as DNA damage responses, replication stress adaptation, and maintenance of transcriptional fidelity. Dysregulation of Kdm5a/RBP2 activity has been linked to altered developmental trajectories and disease-relevant phenotypes in models of cancer biology, neurodevelopment, and stem cell function through perturbation of chromatin-based gene control.
RBP2 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Kdm5a upregulation across a broader range of human cell types.
RBP2 Lentiviral Activation Particles (m) 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 Kdm5a transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous RBP2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Kdm5a 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.