The DPP7 Knockout A2780 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human A2780 epithelial ovarian carcinoma cell line. This knockout model features targeted disruption of the DPP7 gene, which encodes dipeptidyl peptidase 7, a lysosomal serine protease. The polyclonal population provides a heterogeneous loss-of-function system suitable for studying DPP7-dependent processes without the clonal selection artifacts associated with single-cell-derived lines. Researchers can utilize these cells to dissect the functional contributions of DPP7 in ovarian cancer cell biology.
The A2780 cell line is a well-characterized human ovarian carcinoma model originally derived from an untreated patient. It is extensively employed in drug sensitivity studies, particularly for evaluating platinum-based chemotherapeutics such as cisplatin. A2780 cells retain key molecular features of epithelial ovarian cancer, including p53 wild-type status and intact apoptotic signaling, making them a valuable substrate for investigating chemoresistance mechanisms and tumor suppressor pathways.
DPP7 functions as a lysosomal exopeptidase that specifically cleaves N-terminal X-Pro dipeptides from peptide substrates. This proteolytic activity contributes to terminal protein degradation and regulates the processing of pro-apoptotic substrates. DPP7 is transcriptionally regulated by p53 and E2F1 in response to quiescence signals, placing it at the intersection of cell-cycle control and apoptosis. Downstream, DPP7 modulates the availability of pro-apoptotic proteins and affects the processing of chemokines such as CXCL10, thereby linking lysosomal proteolysis to immune signaling. Interacting factors include various lysosomal hydrolases and substrate proteins that traffic to the lysosome.
In the A2780 ovarian cancer context, knockout of DPP7 is expected to impair the cleavage of pro-apoptotic substrates, potentially desensitizing cells to intrinsic apoptotic stimuli. This alteration may contribute to enhanced chemoresistance, a critical barrier in ovarian cancer therapy. The model enables the study of how lysosomal protease activity influences quiescence regulation and drug response, offering insights into mechanisms that promote tumor cell survival under therapeutic stress.
These polyclonal knockout cells are suited for a range of research applications, including investigating DPP7’s role in apoptosis and chemosensitivity. Typical assays include western blotting to confirm DPP7 protein loss, fluorometric protease activity assays, apoptosis detection via Annexin V staining, cell viability assays (e.g., MTT), RT-qPCR for DPP7 mRNA quantification, cisplatin-based chemosensitivity testing, and immunofluorescence for lysosomal localization. For further information, please contact Ascent Research.
