
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
GRP94 Lentiviral Activation Particles (m) | sc-423491-LAC | 200 µl | $455.00 |
Mouse Hsp90b1 encodes GRP94 (gp96), an endoplasmic reticulum (ER) HSP90-family chaperone that supports proteostasis by facilitating folding and quality control of secreted and membrane proteins, including integrins and multiple immune receptors. GRP94 participates in the unfolded protein response (UPR) and ER-associated degradation (ERAD), linking ER stress signaling to calcium homeostasis and secretory pathway function. Because GRP94 influences antigen presentation, innate immune signaling, and cell-surface receptor maturation, altered Hsp90b1 activity is frequently studied in contexts of inflammation, immune dysregulation, and stress-adaptive programs relevant to tumor biology.
GRP94 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Hsp90b1 upregulation across a broader range of human cell types.
GRP94 Lentiviral Activation Particles (m) 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 Hsp90b1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous GRP94 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Hsp90b1 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.