NIPBL Lentiviral Activation Particles (h): sc-403371-LAC

NIPBL (Nipped-B-like protein) encodes a cohesin-loading factor that coordinates sister chromatid cohesion and higher-order chromatin organization, enabling accurate chromosome segregation and DNA damage responses. By facilitating cohesin deposition and stabilizing long-range enhancer–promoter contacts, NIPBL influences genome-wide transcriptional programs critical for embryonic development and cell fate decisions. NIPBL-dependent regulation intersects with pathways controlling replication timing, transcriptional elongation, and repair of double-strand breaks. Dysregulation of NIPBL function is associated with cohesinopathies such as Cornelia de Lange syndrome and has been studied in the context of chromatin architecture changes observed in cancer and neurodevelopmental disorders.

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

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