PGD synthase Lentiviral Activation Particles (h): sc-405437-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PGD synthase Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- PGD synthase Lentiviral Activation Particles (h) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
- Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
- gRNAs encoded by PGD synthase Lentiviral Activation Plasmid (h) and PGD synthase Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the HPGDS promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PGD synthase Lentiviral Activation Particles (h) | sc-405437-LAC | 200 µl | $455.00 | |||
PGD synthase Lentiviral Activation Particles (h2) | sc-405437-LAC-2 | 200 µl | $455.00 |
Human HPGDS encodes hematopoietic prostaglandin D synthase (PGD synthase), a glutathione-dependent enzyme that converts prostaglandin H2 to prostaglandin D2 within the arachidonic acid and eicosanoid biosynthesis network. PGD2 and its downstream metabolites regulate leukocyte chemotaxis, cytokine signaling, vascular tone, and lipid mediator class switching, linking HPGDS activity to immune and inflammatory processes. HPGDS expression is prominent in mast cells and other hematopoietic lineages and is commonly studied in the context of allergic inflammation, asthma, and broader inflammatory disease mechanisms. Because PGD2 signaling engages DP1/DP2 receptor pathways and intersects with oxidative stress and leukotriene/prostaglandin balance, HPGDS serves as a useful node for dissecting lipid mediator–driven transcriptional programs.
PGD synthase 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 HPGDS upregulation across a broader range of human cell types.
PGD synthase 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 HPGDS transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PGD synthase expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native HPGDS 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.