Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
DnaJC3 Lentiviral Activation Particles (h): sc-405100-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- DnaJC3 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
- DnaJC3 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 DnaJC3 Lentiviral Activation Plasmid (h) and DnaJC3 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the DNAJC3 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: DnaJC3 Antibody (A-7): sc-393559
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
DnaJC3 Lentiviral Activation Particles (h) | sc-405100-LAC | 200 µl | $455.00 |
DNAJC3 encodes the ER-resident co-chaperone DnaJC3 (also known as p58IPK), a member of the Hsp40/DnaJ family that modulates protein homeostasis during endoplasmic reticulum stress. DnaJC3 participates in the unfolded protein response and attenuates stress-linked signaling by interacting with PERK/EIF2AK3 and other regulators of translation and chaperone activity, thereby shaping proteostasis, ER-associated degradation, and cellular adaptation to misfolded proteins. Altered DNAJC3 function has been associated with dysregulated stress signaling and proteotoxic vulnerability, with relevance to metabolic and neurodegenerative phenotypes reported in genetic and mechanistic studies. These properties make DNAJC3 a useful node for dissecting ER stress circuitry, translational control, and crosstalk between UPR signaling and inflammatory pathways in human cell models.
DnaJC3 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 DNAJC3 upregulation across a broader range of human cell types.
DnaJC3 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 DNAJC3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous DnaJC3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native DNAJC3 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.