Dyrk1A Lentiviral Activation Particles (h): sc-401928-LAC

DYRK1A encodes dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A), a serine/threonine kinase that autophosphorylates on tyrosine and modulates phosphorylation of diverse nuclear and cytoplasmic substrates. Dyrk1A contributes to cell-cycle control, neuronal differentiation, synaptic function, and proteostasis through regulation of transcription factors, splicing components, and signaling intermediates, intersecting with pathways such as MAPK/ERK, NFAT-dependent transcription, and ribosome/translation control. Altered DYRK1A dosage is strongly implicated in neurodevelopmental phenotypes, including those associated with trisomy 21, and variants are linked to intellectual disability and autism spectrum–related traits. Dysregulated DYRK1A activity has also been studied in the context of tumor biology and neurodegeneration-relevant phosphorylation networks.

Dyrk1A 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 DYRK1A upregulation across a broader range of human cell types.

Dyrk1A 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 DYRK1A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Dyrk1A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native DYRK1A 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.