The ELANE Knockout SK-OV-3 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout population derived from the human SK-OV-3 ovarian adenocarcinoma line. This model features targeted disruption of ELANE, encoding neutrophil elastase, a serine protease key in extracellular matrix degradation and inflammatory signaling. The polyclonal format provides a heterogeneous loss-of-function pool for robust phenotype assessment without clonal selection pressures, enabling study of protease-independent mechanisms in a cancer-relevant background.
SK-OV-3 is a widely used epithelial ovarian adenocarcinoma cell line isolated from ascites, characterized by p53 deficiency and resistance to cisplatin and doxorubicin. It exhibits tumorigenic and metastatic properties in vivo with an epithelial morphology suitable for standard assays. This drug-resistant background provides a clinically relevant system to investigate ELANE loss-of-function effects on tumor cell behavior, particularly extracellular matrix interactions and inflammatory responses.
ELANE encodes a serine protease released during neutrophil degranulation, degrading elastin, fibronectin, and other ECM components, and participating in NETosis and host defense. In ovarian cancer, tumor or infiltrating immune cell-derived ELANE influences the microenvironment. Its activity is regulated by upstream factors G-CSF, C/EBP??, and NF-??B, and proteolytic release of cytokines activates downstream targets like MMP9, TLR4, and TGF-??. ELANE is inhibited by ??1-antitrypsin (SERPINA1), SLPI, and elafin, and its interplay with inhibitors and receptors such as integrins and TLR4 determines net proteolytic and signaling outputs.
Knocking out ELANE in SK-OV-3 eliminates endogenous neutrophil elastase activity, disentangling protease-dependent from protease-independent functions. This clean background facilitates dissection of ELANE??s roles in ECM remodeling, cytokine signaling, and metastasis without endogenous protease interference. The model is valuable for studying ELANE-driven tumor?Cstroma interactions, inflammation-mediated progression, and drug response in a p53-deficient, chemoresistant ovarian cancer setting. It also supports complementation with ELANE variants for structure?Cfunction analysis.
Applications include investigating tumor microenvironment remodeling, serine protease roles in ovarian cancer invasion, NETosis in cancer, and screening elastase inhibitors. Compatible assays comprise immunoblotting for ELANE, elastase activity measurement, ECM degradation, multiplex cytokine profiling, and migration/invasion studies. Sanger sequencing and RT-qPCR confirm target disruption. These polyclonal knockout cells serve as controls for ELANE expression studies. For additional information or custom applications, contact Ascent Research.
