YB-1 Lentiviral Activation Particles (h): sc-401385-LAC

YBX1 encodes Y-box binding protein 1 (YB-1), an RNA/DNA-binding regulator that coordinates transcription, mRNA splicing, stabilization, and translation in response to cellular stress. YB-1 participates in pathways linked to cell-cycle control, DNA damage responses, and remodeling of ribonucleoprotein complexes, influencing processes such as proliferation, apoptosis, and epithelial–mesenchymal transition. Dysregulated YBX1/YB-1 activity has been associated with oncogenic signaling networks, drug resistance phenotypes, and inflammatory and fibrotic programs, making it a widely studied node in tumor biology and stress-adaptation mechanisms. As a multifunctional nucleic acid–binding protein, YB-1 is frequently investigated for its roles in post-transcriptional gene regulation and transcription factor crosstalk.

YB-1 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 YBX1 upregulation across a broader range of human cell types.

YB-1 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 YBX1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous YB-1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native YBX1 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.