TIMP-1 Lentiviral Activation Particles (h): sc-400408-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- TIMP-1 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
- TIMP-1 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 TIMP-1 Lentiviral Activation Plasmid (h) and TIMP-1 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the TIMP1 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: TIMP-1 Antibody (G-6): sc-365905
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
TIMP-1 Lentiviral Activation Particles (h) | sc-400408-LAC | 200 µl | $455.00 | |||
TIMP-1 Lentiviral Activation Particles (h2) | sc-400408-LAC-2 | 200 µl | $455.00 |
TIMP1 encodes tissue inhibitor of metalloproteinases-1 (TIMP-1), a secreted glycoprotein that binds and inhibits multiple matrix metalloproteinases to regulate extracellular matrix (ECM) turnover and pericellular proteolysis. By modulating MMP activity, TIMP-1 influences cell migration, adhesion, and tissue remodeling, processes that intersect with inflammatory signaling, angiogenic programs, and wound-healing responses. TIMP-1 also participates in protease–inhibitor balance that shapes ECM-dependent signaling and can affect cytokine availability and growth factor bioactivity. Dysregulated TIMP1 expression has been associated with fibrosis, neuroinflammatory contexts, and tumor microenvironment remodeling, supporting its use in mechanistic studies of ECM dynamics and cell–matrix interactions.
TIMP-1 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 TIMP1 upregulation across a broader range of human cell types.
TIMP-1 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 TIMP1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TIMP-1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TIMP1 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.