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.
HSP 90α Double Nickase Plasmid (m): sc-420981-NIC
- Target species: mouse
- 20 µg of transfection-ready, purified plasmid DNA; Suitable for up to 20 transfections
- HSP 90α Double Nickase Plasmid (m) consists of a pair of plasmids each encoding a D10A mutated Cas9 nuclease and a target-specific 20 nt guide RNA (gRNA) designed to knockout gene expression with greater specificity than its CRISPR/Cas9 KO counterpart
- Paired gRNA sequences are offset by approximately 20 bp to allow for specific Cas9-mediated double nicking of the genomic DNA, which mimics a DSB
- One plasmid in the pair contains a puromycin-resistance gene for selection; the other plasmid in the pair contains a GFP marker to visually confirm transfection
- HSP 90α Double Nickase Plasmid (m) and HSP 90α Double Nickase Plasmid (m2) encode distinct paired gRNA designs targeting Hsp90aa1. One or both designs may be available
- Following transfection, gene knockout efficiency can be assayed by WB, IF or IHC using antibody: HSP 90α Antibody (F-2): sc-515081
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
HSP 90α Double Nickase Plasmid (m) | sc-420981-NIC | 20 µg | $410.00 | |||
HSP 90α Double Nickase Plasmid (m2) | sc-420981-NIC-2 | 20 µg | $410.00 |
Mouse Hsp90aa1 encodes the inducible cytosolic chaperone HSP 90α, a central component of the proteostasis network that stabilizes and matures a broad range of client proteins, including kinases, steroid receptors, and transcription factors. HSP 90α cooperates with co-chaperones such as CDC37 and the HSP70 machinery to regulate protein folding, quality control, and stress-responsive remodeling of signaling complexes. Through these interactions it influences pathways including MAPK/ERK, PI3K–AKT, and steroid hormone signaling, impacting cell-cycle progression, apoptosis, and responses to proteotoxic stress. Dysregulated HSP90α-dependent chaperoning has been linked to altered signaling robustness and protein homeostasis in models of cancer biology, neurodegeneration, and inflammatory stress.
HSP 90α Double Nickase Plasmid (m) consists of a matched pair of plasmids engineered for high-specificity editing of the Hsp90aa1 locus in mouse cell lines. Each plasmid expresses a Cas9 D10A nickase and a distinct sgRNA targeting opposite DNA strands within Hsp90aa1. When directed to adjacent sites on opposite DNA strands, the two nickases generate offset single-strand nicks that together produce a staggered double-strand break, requiring coordinated on-target activity from both guides. The resulting DNA break is resolved by endogenous cellular repair pathways, most commonly through non-homologous end joining (NHEJ), leading to insertions or deletions that disrupt Hsp90aa1 function. By requiring dual sgRNA engagement at the target locus, the double nicking approach enhances editing specificity and provides a complementary CRISPR strategy for applications where additional control over targeting precision is desired.
To support efficient identification of edited cells, one plasmid encodes GFP for fluorescent visualization of transfected populations, while the companion plasmid carries a puromycin resistance gene for antibiotic selection. Together, these features support efficient enrichment of co-transfected populations and simplify the validation of Hsp90aa1-disrupted clones.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.