The DNAJC7 Knockout SK-HEP-1 Polyclonal Cells product consists of a CRISPR/Cas9-edited polyclonal knockout cell population derived from the SK-HEP-1 human hepatic adenocarcinoma cell line. In this model, the gene encoding DNAJC7, a tetratricopeptide repeat-containing co-chaperone, has been disrupted via CRISPR/Cas9-mediated gene editing, generating a heterogeneous pool of cells carrying diverse loss-of-function alleles. This polyclonal population provides a robust loss-of-function system for studying DNAJC7-dependent processes without the need for isolation of single-cell clones, offering a practical tool for functional genomics and drug discovery applications.
The host cell line, SK-HEP-1, is a widely used model of hepatocellular carcinoma originally isolated from the ascitic fluid of a male patient with liver adenocarcinoma. These malignant liver epithelial cells retain characteristic features of hepatic cancer cells, including dysregulated proliferative signaling and altered metabolic pathways, making them particularly suitable for investigating oncogenic mechanisms and therapeutic vulnerabilities. SK-HEP-1 cells are known to express components of the molecular chaperone network, providing a relevant background for probing the function of co-chaperones like DNAJC7 in liver cancer biology.
DNAJC7 functions as a critical co-chaperone that recruits Hsp70 and Hsp90 to modulate the folding, maturation, and turnover of client proteins, thereby maintaining proteostasis under basal and stress conditions. It physically interacts with Hsp70, Hsp90, and the E3 ubiquitin ligase STUB1/CHIP, facilitating either productive folding or targeting of terminally misfolded clients for degradation via the ubiquitin-proteasome system. DNAJC7 expression is induced by heat shock factor 1 (HSF1) in response to cellular stress, linking it to the heat shock response and proteotoxic stress pathways. Downstream, the absence of DNAJC7 is expected to impair the handling of a broad range of Hsp70 and Hsp90 client proteins, potentially shifting the balance toward protein misfolding and aggregation.
In the context of SK-HEP-1 hepatocellular carcinoma cells, loss of DNAJC7-mediated protein quality control may have profound effects on tumor cell homeostasis. Cancer cells frequently depend on upregulated chaperone machinery to survive oncogenic stress, and disruption of co-chaperone networks can sensitize tumor cells to proteasome inhibitors or other stress-inducing agents. This polyclonal knockout model thus enables investigation of how DNAJC7 contributes to stress adaptation, protein folding fidelity, and viability in liver cancer, offering a platform to explore proteostasis-targeting therapeutic strategies.
Researchers can employ this knockout pool in a variety of experimental workflows, including western blotting to monitor Hsp70 and Hsp90 client protein levels, RT-qPCR profiling of HSF1-driven stress response genes, co-immunoprecipitation to assess alterations in chaperone complexes, proteasome activity assays, and heat shock challenge experiments coupled with viability measurements. These approaches enable detailed dissection of co-chaperone function and chaperone-mediated proteostasis in hepatocellular carcinoma. Additional applications include drug screening for modulators of chaperone activity and genetic interaction studies. For further information, please contact Ascent Research.
