SRPK1 Lentiviral Activation Particles (h): sc-402855-LAC

Human SRPK1 (serine/arginine-rich protein-specific kinase 1) is a conserved serine/threonine kinase that phosphorylates SR splicing factors, coordinating spliceosome assembly and regulating alternative pre-mRNA splicing. By controlling phosphorylation-dependent nucleo-cytoplasmic trafficking and activity of splicing regulators, SRPK1 integrates signaling inputs with RNA processing programs that influence cell-cycle progression, stress responses, and gene-expression fidelity. Altered SRPK1 activity and SR protein phosphorylation patterns have been associated with dysregulated splicing networks observed in cancer biology, angiogenic signaling, and neurodegeneration-relevant RNA processing phenotypes. As a pathway node linking kinase signaling to transcript isoform selection, SRPK1 is frequently studied in mechanisms of splicing control, proteomic phosphoregulation, and isoform-resolved functional genomics.

SRPK1 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 SRPK1 upregulation across a broader range of human cell types.

SRPK1 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 SRPK1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SRPK1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SRPK1 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.