DNAJC7 Knockout A2780 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal population derived from A2780 human ovarian adenocarcinoma cells, providing a loss-of-function model for the DNAJC7 co-chaperone gene. The polyclonal pool harbors targeted disruptions in DNAJC7, generating a heterogeneous knockout population ideal for studying chaperone biology without clonal selection.
The A2780 host cell line is an established model of epithelial ovarian adenocarcinoma, originally isolated from an untreated patient. These cells exhibit epithelial morphology and are widely utilized in ovarian cancer research, particularly for investigating drug sensitivity and resistance mechanisms, as well as apoptotic signaling. The A2780 cell line retains key features of ovarian cancer, including responsiveness to platinum-based chemotherapeutics, making it a valuable platform for studying molecular determinants of treatment response. By employing A2780 as the parental line, the DNAJC7 knockout population enables dissection of co-chaperone functions specifically within the ovarian cancer context.
DNAJC7 is a J-domain co-chaperone that stimulates ATP hydrolysis by Hsp70 chaperones HSPA1A and HSPA8, driving client protein folding, refolding, or degradation. It interacts with the E3 ligase STUB1 to direct misfolded proteins to the ubiquitin-proteasome system. Transcription of DNAJC7 is activated by HSF1 under stress. Knockout impairs Hsp70 activity, causing misfolded protein accumulation and altered apoptosis via the unfolded protein response.
In A2780 ovarian adenocarcinoma cells, DNAJC7 knockout likely compromises the protein quality control network, which is critical for coping with proteotoxic stress often heightened in cancer cells. Given the reliance of cancer cells on chaperone systems for survival under adverse conditions, loss of DNAJC7 may sensitize A2780 cells to proteasome inhibitors or enhance apoptotic responses to chemotherapeutic agents. This model thus enables exploration of how co-chaperone-mediated regulation of Hsp70 contributes to ovarian cancer cell viability, drug resistance, and stress adaptation, providing a relevant platform for mechanistic studies in a disease-relevant epithelial cell background.
This polyclonal population enables western blotting, RT-qPCR, co-immunoprecipitation, apoptosis assays, drug sensitivity testing, and protein aggregation assays. Research applications include studying chaperone-mediated protein quality control, Hsp70 co-chaperone roles in ovarian cancer drug resistance, apoptosis signaling, and stress response pathways. For further details or ordering information, please contact Ascent Research.
