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.
GM130 Lentiviral Activation Particles (h): sc-400787-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- GM130 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
- GM130 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 GM130 Lentiviral Activation Plasmid (h) and GM130 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the GOLGA2 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: GM130 Antibody (H-7): sc-55590
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
GM130 Lentiviral Activation Particles (h) | sc-400787-LAC | 200 µl | $455.00 |
GOLGA2 encodes the cis-Golgi matrix protein GM130, a peripheral membrane tethering factor that helps organize Golgi ribbon architecture and maintain stacked cisternae. GM130 coordinates vesicle capture and fusion through interactions with p115/USO1 and other golgins, supports COPI/COPII-dependent trafficking, and contributes to centrosome positioning, microtubule organization, and cell polarity. Through its roles in secretory pathway flux and Golgi integrity, altered GM130 function is relevant to cellular stress responses, migration, and phenotypes observed in proliferative and neurodegenerative disease models where Golgi fragmentation and trafficking imbalance are common. These processes make GOLGA2 a useful node for studying membrane trafficking, organelle biogenesis, and signaling linked to proteostasis and cell-cycle control.
GM130 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 GOLGA2 upregulation across a broader range of human cell types.
GM130 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 GOLGA2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous GM130 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native GOLGA2 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.