HSP70-1 Lentiviral Activation Particles (h): sc-418088-LAC

HSPA1A encodes the inducible molecular chaperone HSP70-1, a central component of the cellular heat shock response that preserves proteostasis by assisting nascent protein folding, preventing aggregation, and promoting refolding or triage of damaged proteins. HSP70-1 cooperates with co-chaperones and the ubiquitin–proteasome and autophagy pathways to regulate protein quality control during oxidative stress, proteotoxic stress, and inflammation. Through modulation of stress signaling, apoptosis, and antigen processing, HSPA1A activity influences cellular adaptation in contexts such as neurodegeneration, ischemic injury, and oncogenic stress without implying clinical benefit. Its rapid inducibility also makes it a useful readout and regulator in studies of stress granules, ER stress crosstalk, and cytoprotection pathways.

HSP70-1 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 HSPA1A upregulation across a broader range of human cell types.

HSP70-1 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 HSPA1A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HSP70-1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HSPA1A 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.