matrin-3 Lentiviral Activation Particles (h): sc-418085-LAC

MATR3 encodes matrin-3, a nuclear matrix RNA/DNA-binding protein implicated in organizing nuclear architecture and regulating gene expression programs through RNA processing, stabilization, and nucleocytoplasmic transport. Matrin-3 associates with ribonucleoprotein complexes and influences pre-mRNA splicing and transcriptional regulation, linking it to pathways governing genome maintenance and stress-responsive RNA metabolism. Dysregulation or mutation of MATR3 has been connected to neurodegenerative phenotypes, including ALS and distal myopathy, highlighting its relevance to studies of neuronal homeostasis and RNA-binding protein biology. As a broadly expressed nuclear factor, matrin-3 is frequently examined in the context of proteostasis, phase-separated RNP assemblies, and cell-type–specific vulnerability to RNA processing defects.

matrin-3 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 MATR3 upregulation across a broader range of human cell types.

matrin-3 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 MATR3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous matrin-3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native MATR3 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.