CENP-F Lentiviral Activation Particles (h): sc-402178-LAC

CENPF encodes CENP-F, a large centromere-kinetochore–associated protein that accumulates during late G2 and peaks in mitosis to coordinate chromosome alignment, spindle checkpoint signaling, and faithful sister chromatid segregation. CENP-F participates in kinetochore–microtubule attachment dynamics and links mitotic progression to nuclear envelope and microtubule organization, supporting orderly cell-cycle transitions. Altered CENPF expression is frequently associated with proliferative phenotypes and chromosomal instability, making it relevant to studies of aneuploidy, genome maintenance, and tumor cell biology. In human cells, perturbation of CENP-F impacts mitotic timing and chromosome congression pathways that are commonly interrogated in cell-cycle and cancer research.

CENP-F 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 CENPF upregulation across a broader range of human cell types.

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