hnRNP A0 Lentiviral Activation Particles (h): sc-406924-LAC

HNRNPA0 encodes hnRNP A0, an RNA-binding protein that associates with mRNP complexes to regulate post-transcriptional gene expression, including mRNA stability, turnover, and translation of select transcripts. Through these functions it contributes to cellular stress responses and dynamic remodeling of gene expression programs that impact cell-cycle control and inflammatory signaling. hnRNP A0 has been studied in the context of kinase-driven signaling networks and RNA metabolism pathways that shape transcript fate under stress conditions. Dysregulation of hnRNP family proteins and associated RNA-processing mechanisms is frequently linked to altered proliferative and stress-adaptation phenotypes relevant to cancer biology and other disorders involving aberrant gene expression.

hnRNP A0 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 HNRNPA0 upregulation across a broader range of human cell types.

hnRNP A0 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 HNRNPA0 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous hnRNP A0 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HNRNPA0 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.