HSPA5/BiP/GRP78 Lentiviral Activation Particles (h): sc-400073-LAC

HSPA5 encodes BiP/GRP78, an endoplasmic reticulum (ER) HSP70 family chaperone that binds nascent polypeptides and regulates protein folding quality control. As a central sensor of ER homeostasis, HSPA5 modulates the unfolded protein response (UPR) through interactions that influence PERK, IRE1, and ATF6 signaling, linking proteostasis to ER-associated degradation, calcium handling, and oxidative stress responses. Dysregulated HSPA5 activity is commonly studied in contexts of chronic ER stress, including cancer cell adaptation, metabolic disease, and neurodegeneration, where altered proteostasis and UPR signaling contribute to cellular survival and inflammatory pathways. Because BiP/GRP78 affects secretion and membrane protein maturation, it is also relevant to studies of viral protein processing and host–pathogen interactions.

HSPA5/BiP/GRP78 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 HSPA5 upregulation across a broader range of human cell types.

HSPA5/BiP/GRP78 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 HSPA5 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HSPA5/BiP/GRP78 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HSPA5 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.