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.
Titin Lentiviral Activation Particles (h): sc-402827-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- Titin 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
- Titin 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 Titin Lentiviral Activation Plasmid (h) and Titin Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the TTN promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: Titin Antibody (E-2): sc-271946
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
Titin Lentiviral Activation Particles (h) | sc-402827-LAC | 200 µl | $455.00 |
Human TTN encodes titin, a giant sarcomeric scaffold protein that spans the Z-disc to M-line and integrates mechanical elasticity with myofibril architecture. Titin organizes thick filament positioning, contributes to passive tension via extensible I-band domains, and coordinates mechanosensitive signaling at the Z-disc and M-band through interactions with proteins such as telethonin, obscurin, and muscle-specific kinase hubs. Through its roles in sarcomere assembly, force transmission, and protein quality control, TTN influences pathways including mechanotransduction, ubiquitin–proteasome turnover, and stress-adaptive remodeling in striated muscle. Genetic and functional perturbation of TTN is strongly associated with cardiomyopathies and skeletal myopathies, making titin regulation a key focus in muscle biology and disease modeling.
Titin 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 TTN upregulation across a broader range of human cell types.
Titin 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 TTN transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Titin expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TTN 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.