HSP70-2 Lentiviral Activation Particles (h): sc-417733-LAC

HSPA1B encodes the inducible chaperone HSP70-2, a central component of the cellular heat shock response that safeguards proteostasis during thermal, oxidative, and inflammatory stress. HSP70-2 binds exposed hydrophobic regions on nascent or misfolded proteins to prevent aggregation and supports refolding in coordination with HSP40/DNAJ co-chaperones and nucleotide exchange factors. Through roles in protein quality control, unfolded protein response crosstalk, and regulation of apoptosis and innate immune signaling, HSP70-2 influences cell survival decisions under stress. Dysregulated HSP70 family activity has been associated with proteotoxic and inflammatory states, making HSPA1B a useful target for mechanistic studies of stress-adaptation pathways.

HSP70-2 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 HSPA1B upregulation across a broader range of human cell types.

HSP70-2 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 HSPA1B transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HSP70-2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HSPA1B 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.