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.
SPOP Lentiviral Activation Particles (h): sc-401290-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- SPOP 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
- SPOP 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 SPOP Lentiviral Activation Plasmid (h) and SPOP Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the SPOP promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: SPOP Antibody (B-8): sc-377206
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
SPOP Lentiviral Activation Particles (h) | sc-401290-LAC | 200 µl | $455.00 |
Human SPOP (speckle-type POZ protein) is a substrate adaptor for the CUL3–RBX1 E3 ubiquitin ligase complex that promotes ubiquitination and proteasome-dependent turnover of diverse nuclear and cytoplasmic proteins. Through regulation of protein stability, SPOP influences transcriptional programs, chromatin-associated processes, DNA damage responses, and signaling networks including androgen receptor and PI3K–AKT pathway components. Perturbation of SPOP-mediated ubiquitin signaling can rewire cellular homeostasis and stress responses, making SPOP a key node for studying proteostasis and pathway cross-talk. Altered SPOP function and substrate recognition have been linked to cancer-associated mechanisms, including dysregulated transcription factor abundance and aberrant signaling output in tumor-relevant contexts.
SPOP 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 SPOP upregulation across a broader range of human cell types.
SPOP 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 SPOP transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SPOP expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SPOP 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.