HSPA8/HSC70 Lentiviral Activation Particles (h): sc-418508-LAC

HSPA8 (HSC70) encodes a constitutively expressed HSP70 family chaperone that supports proteostasis by regulating ATP-dependent protein folding, refolding, and prevention of aggregation. HSC70 coordinates chaperone-mediated autophagy via lysosomal targeting of KFERQ-motif substrates, participates in clathrin-mediated endocytosis, and assists maturation and trafficking of signaling proteins. Through interactions with co-chaperones and the ubiquitin–proteasome system, it influences stress responses, cytoskeletal dynamics, and organelle quality control. Dysregulation of HSPA8-linked chaperone networks has been associated with neurodegeneration, cancer cell survival programs, and host–pathogen interactions, making it a useful node for pathway-focused functional studies.

HSPA8/HSC70 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 HSPA8 upregulation across a broader range of human cell types.

HSPA8/HSC70 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 HSPA8 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HSPA8/HSC70 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HSPA8 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.