CD274/PD-L1 Lentiviral Activation Particles (h): sc-401140-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- CD274/PD-L1 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
- CD274/PD-L1 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 CD274/PD-L1 Lentiviral Activation Plasmid (h) and CD274/PD-L1 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the CD274 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: CD274/PD-L1 Antibody (1C10): sc-293425
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
CD274/PD-L1 Lentiviral Activation Particles (h) | sc-401140-LAC | 200 µl | $455.00 | |||
CD274/PD-L1 Lentiviral Activation Particles (h2) | sc-401140-LAC-2 | 200 µl | $455.00 |
CD274 encodes PD-L1 (CD274), a type I transmembrane immune checkpoint ligand that binds PD-1 (PDCD1) and modulates T cell activation, cytokine production, and peripheral tolerance. PD-L1 expression is induced by inflammatory cues such as IFN-γ via JAK/STAT signaling and can be regulated by oncogenic pathways including PI3K–AKT–mTOR and MAPK, linking immune signaling to cellular stress responses. Through engagement of PD-1, PD-L1 contributes to attenuation of antigen-specific immune responses and shapes the balance between immune surveillance and immune evasion. Aberrant PD-L1 regulation has been associated with immune dysfunction and is widely studied in cancer immunology, chronic infection, and autoimmunity models.
CD274/PD-L1 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 CD274 upregulation across a broader range of human cell types.
CD274/PD-L1 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 CD274 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CD274/PD-L1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CD274 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.