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.
COL12A1 Lentiviral Activation Particles (h): sc-402361-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- COL12A1 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
- COL12A1 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 COL12A1 Lentiviral Activation Plasmid (h) and COL12A1 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the COL12A1 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: COL12A1 Antibody (A-11): sc-166020
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
COL12A1 Lentiviral Activation Particles (h) | sc-402361-LAC | 200 µl | $455.00 |
COL12A1 encodes collagen type XII alpha 1 chain, a fibril-associated collagen with interrupted triple helices (FACIT) that localizes to the extracellular matrix and regulates collagen fibrillogenesis, tissue tensile strength, and mechanotransduction. By organizing collagen I–rich fibrils and interfacing with proteoglycans and cell-surface receptors, COL12A1 contributes to matrix remodeling, cell adhesion, and migration programs that influence development and musculoskeletal homeostasis. Altered COL12A1 expression or function has been linked to heritable connective tissue phenotypes and extracellular matrix dysregulation, making it relevant to studies of tendon/ligament biology, fibrosis, and matrix-driven signaling. These roles position COL12A1 as a useful node for dissecting how ECM architecture shapes cellular behavior and stress responses.
COL12A1 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 COL12A1 upregulation across a broader range of human cell types.
COL12A1 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 COL12A1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous COL12A1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native COL12A1 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.