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.
ATR Lentiviral Activation Particles (h): sc-400335-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- ATR 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
- ATR 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 ATR Lentiviral Activation Plasmid (h) and ATR Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ATR promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: ATR Antibody (C-1): sc-515173
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ATR Lentiviral Activation Particles (h) | sc-400335-LAC | 200 µl | $455.00 |
ATR (ataxia telangiectasia and Rad3-related) encodes a PI3K-like serine/threonine kinase that functions as a central sensor of replication stress and single-stranded DNA, activating checkpoint signaling to preserve genome stability. ATR is recruited via ATRIP and stimulated by TOPBP1 and ETAA1 to phosphorylate key substrates such as CHK1, coordinating S-phase progression, replication fork stabilization, and DNA repair pathway choice. Through crosstalk with homologous recombination factors and fork protection complexes, ATR signaling limits replication-associated double-strand breaks and controls cell-cycle arrest under genotoxic stress. Dysregulated ATR pathway activity is linked to chromosomal instability and is frequently studied in the context of cancer biology, neurodevelopmental disorders, and syndromes involving impaired DNA damage response.
ATR 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 ATR upregulation across a broader range of human cell types.
ATR 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 ATR transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ATR expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ATR 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.