PRP4 kinase Lentiviral Activation Particles (h2): sc-411224-LAC-2
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PRP4 kinase Lentiviral Activation Particles (h2) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- PRP4 kinase Lentiviral Activation Particles (h2) 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 PRP4 kinase Lentiviral Activation Plasmid (h2) and PRP4 kinase Lentiviral Activation Plasmid (h22) target distinct regulatory regions of the PRPF4B promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PRP4 kinase Lentiviral Activation Particles (h2) | sc-411224-LAC-2 | 200 µl | $455.00 |
Human PRPF4B encodes PRP4 kinase, a serine/threonine protein kinase that associates with the U4/U6·U5 tri-snRNP and regulates pre-mRNA splicing by phosphorylating spliceosomal components to support spliceosome assembly and catalytic activation. Through control of splice-site selection and transcript maturation, PRP4 kinase links nuclear RNA processing to cell-cycle progression and stress-responsive signaling programs that depend on coordinated gene expression. Dysregulation of PRPF4B expression or activity has been connected to aberrant splicing patterns observed in cancer and other disorders with altered RNA processing, making it relevant for studies of transcriptome remodeling and proteome diversity. Gene editing of PRPF4B in human cells enables mechanistic interrogation of spliceosome dynamics, phosphoregulation of splicing factors, and downstream impacts on alternative splicing, DNA damage responses, and cellular phenotypes in functional genomics workflows.
PRP4 kinase Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient PRPF4B upregulation across a broader range of human cell types.
PRP4 kinase Lentiviral Activation Particles (h2) 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 PRPF4B transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PRP4 kinase expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PRPF4B 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.