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Panoply™ Human HSP90AA1 Over-expressing Stable Cell Line

For research use only. Not intended for any clinical use.

Cat. No. :   CSC-SC007301

Host Cell :   HEK293 (CHO and other cell types are also available) Size :   >1x106 frozen cells/vial

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Cell Line Information

Cell Culture Information

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Gene Information

Cat. No. CSC-SC007301
Description Using Creative Biogene's proprietary lentiviral vectors, we subclone the target gene into lentivector, generate the lentivirus particles, sequentially infect the cell line HEK293 (other cell types are also available according to your requirements), and select the clones constantly expressing target gene at high level.
Target Gene HSP90AA1
Gene Species Homo sapiens (Human)
Host Cell HEK293 (CHO and other cell types are also available)
Host Cell Species Species varies
Applications

1. Gene expression studies

2. Signaling pathway research

3. Drug screening and toxicology

4. Disease research

Size 2 × 10^6 cells / vial
Stability Validated for at least 10 passages
Quality Control Negative for bacteria, yeast, fungi and mycoplasma.
Storage Liquid nitrogen
Shipping Dry Ice
Revival Rapidly thaw cells in a 37°C water bath. Transfer contents into a tube containing pre-warmed media. Centrifuge cells and seed into a 25 cm2 flask containing pre-warmed media.
Mycoplasma Negative
Format One frozen vial containing millions of cells
Storage Liquid nitrogen
Safety Considerations The following safety precautions should be observed.
1. Use pipette aids to prevent ingestion and keep aerosols down to a minimum.
2. No eating, drinking or smoking while handling the stable line.
3. Wash hands after handling the stable line and before leaving the lab.
4. Decontaminate work surface with disinfectant or 70% ethanol before and after working with stable cells.
5. All waste should be considered hazardous.
6. Dispose of all liquid waste after each experiment and treat with bleach.
Ship Dry ice
Gene Name HSP90AA1 heat shock protein 90kDa alpha (cytosolic), class A member 1 [ Homo sapiens ]
Gene Symbol HSP90AA1
Synonyms HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4
Gene Description heat shock protein 90kDa alpha (cytosolic), class A member 1
GeneID 3320
Uni ProtID P07900
mRNA Refseq NM_001017963.2
Protein Refseq NP_001017963.2
Chromosome Location 14q32.33
Function ATP binding; ATPase activity; TPR domain binding; TPR domain binding; identical protein binding; nitric-oxide synthase regulator activity; nucleotide binding; protein binding; protein homodimerization activity; unfolded protein binding;
Pathway Antigen processing and presentation, organism-specific biosystem; Antigen processing and presentation, conserved biosystem; Axon guidance, organism-specific biosystem; Cell Cycle, organism-specific biosystem; Cell Cycle, Mitotic, organism-specific biosystem; Centrosome maturation, organism-specific biosystem; Class I PI3K signaling events, organism-specific biosystem;
MIM 140571
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Recent studies have shown that heat shock protein 90 alpha family class A member 1 (HSP90AA1) interacts with various tumor-related proteins, regulating their biological activity and stability, and plays an important role in various cancers. However, the role of HSP90AA1 in clear cell renal cell carcinoma (ccRCC) remains unclear. Here, researchers demonstrated that HSP90AA1 is significantly downregulated in ccRCC, and its reduced expression is associated with tumor metastasis. Overexpression of HSP90AA1 significantly inhibited the proliferation and metastasis of ccRCC cells. HSP90AA1 binds to F-box protein 7 (FBXO7) and promotes its protein expression. FBXO7 is downregulated in ccRCC, and its reduced expression is closely associated with unfavorable pathological features and poor prognosis in patients. Overexpression of FBXO7 promotes the expression of cell adhesion molecule 1 (CADM1) and inhibits the PI3K-AKT signaling pathway. Knocking down FBXO7 expression in the context of HSP90AA1 overexpression significantly reversed the inhibitory effect on cell phenotype caused by HSP90AA1 overexpression, downregulated CADM1 expression, and activated the PI3K-AKT signaling pathway. In summary, HSP90AA1 is downregulated in ccRCC, and HSP90AA1 overexpression promotes CADM1 expression and inhibits the PI3K-AKT pathway, thereby suppressing the proliferation and metastasis of ccRCC.

Here, researchers constructed HSP90AA1-overexpressing OSRC2 and Caki-1 cell lines (Figure 1F). Plate cloning assays showed that the growth ability of HSP90AA1-overexpressing cells was significantly reduced compared to the control group (Figure 1A). EdU and TUNEL fluorescence detection results showed that after HSP90AA1 overexpression, ccRCC cell proliferation was significantly reduced, and the number of apoptotic cells significantly increased (Figure 1B). Cell migration and invasion experiments also showed that HSP90AA1 overexpression significantly inhibited the invasive ability of ccRCC cells (Figure 1C, D). Furthermore, researchers constructed a mouse renal orthotopic xenograft tumor growth model by injecting control or HSP90AA1-overexpressing Caki-1 cells under the renal capsule of mice. Bioluminescence imaging data analysis confirmed that the renal tumor growth rate in the HSP90AA1 overexpression group was significantly lower than that in the control group (Figure 1E). Then, H&E staining was used to detect the pathological structure of the mouse renal tumors (Figure 1F). Subsequently, cell proliferation and apoptosis in the renal tumors were detected using EdU and TUNEL methods, respectively. Compared with the control group, EdU expression was significantly reduced in the HSP90AA1 overexpression group, while TUNEL and Cleaved-Caspase 3 expression were significantly increased. These results fully demonstrate the inhibitory effect of HSP90AA1 overexpression on ccRCC cell proliferation and metastasis.

Figure 1. HSP90AA1 overexpression inhibited the proliferation and metastasis of ccRCC cells in vitro and in vivo.Figure 1. HSP90AA1 overexpression inhibited the proliferation and metastasis of ccRCC cells in vitro and in vivo. (Yang W, et al., 2026)

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