FKBPL Lentiviral Activation Particles (h): sc-410504-LAC

Human FKBPL encodes FK506-binding protein-like (FKBPL), an atypical immunophilin that functions as an HSP90 co-chaperone and scaffolding regulator of signaling proteins involved in proteostasis, cell-cycle control, and stress responses. Through chaperone-dependent mechanisms, FKBPL influences protein folding and stability and has been linked to regulation of steroid receptor signaling and pathways connected to NF-κB–mediated inflammatory responses. Altered FKBPL expression has been reported across multiple disease contexts, including cancer-associated phenotypes such as proliferation, DNA damage responses, and angiogenesis-related programs, supporting its use as a mechanistic node in pathway interrogation. These features make FKBPL a relevant target for dissecting chaperone networks, transcriptional regulation, and context-dependent stress signaling in human cell models.

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

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