KIF20A Lentiviral Activation Particles (h): sc-403194-LAC

KIF20A (kinesin family member 20A; MKLP2) is a microtubule-based motor protein required for mitotic progression, with key roles in spindle organization, chromosome segregation, and cytokinesis. It coordinates central spindle/midbody dynamics and is functionally linked to cell-cycle regulatory networks, including Aurora B–dependent signaling and RhoA-driven contractile ring formation. Dysregulated KIF20A expression has been associated with proliferative phenotypes and altered mitotic fidelity in multiple cancer contexts, making it a useful node for studying cell division stress and genomic instability. Experimental modulation of KIF20A supports interrogation of mitotic exit, abscission timing, and microtubule–actin cross-talk in human cell models.

KIF20A 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 KIF20A upregulation across a broader range of human cell types.

KIF20A 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 KIF20A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous KIF20A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native KIF20A 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.