T-type Ca++ CP α1G Lentiviral Activation Particles (h): sc-418331-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- T-type Ca++ CP α1G 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
- T-type Ca++ CP α1G 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 T-type Ca++ CP α1G Lentiviral Activation Plasmid (h) and T-type Ca++ CP α1G Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the CACNA1G promoter. One or both designs may be available
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
T-type Ca++ CP α1G Lentiviral Activation Particles (h) | sc-418331-LAC | 200 µl | $455.00 |
CACNA1G encodes the human T-type calcium channel α1G (Cav3.1), a low-voltage–activated channel that supports transient Ca²⁺ influx near resting membrane potentials. By shaping membrane excitability, rebound bursting, and oscillatory firing, Cav3.1 influences neuronal and cardiac electrophysiology and couples electrical activity to calcium-dependent signaling, including calmodulin-regulated pathways and downstream transcriptional programs. Altered CACNA1G activity has been associated with disorders involving abnormal rhythmicity and excitability, including seizure susceptibility and cardiac conduction phenotypes, and it is frequently studied in contexts of calcium signaling dysregulation. As a membrane ion channel, CACNA1G also provides a mechanistic link between stimulus-dependent Ca²⁺ entry and cellular processes such as neurotransmitter release, pacemaking, and activity-dependent gene expression.
T-type Ca++ CP α1G 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 CACNA1G upregulation across a broader range of human cell types.
T-type Ca++ CP α1G 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 CACNA1G transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous T-type Ca++ CP α1G expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CACNA1G 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.