EDIL3 Knockout HeLa Polyclonal Cells are a population of HeLa cells that have undergone CRISPR/Cas9-mediated gene disruption of the EDIL3 locus, resulting in a polyclonal knockout model with heterogeneous loss-of-function mutations. This pooled format preserves the genetic diversity of edited cells, enabling studies of EDIL3 deficiency across a range of clonal backgrounds without bias from single-clone artifacts. The product is supplied as a polyclonal knockout cell population suitable for immediate use in functional assays, signaling studies, and xenograft models.
The parental HeLa cell line is an HPV-18 positive cervical adenocarcinoma line established in 1951, widely employed in cancer research, drug screening, and mechanistic studies. These cells exhibit robust proliferation, high transfectability, and well-characterized integrin expression profiles, making them a relevant model for investigating EDIL3-mediated adhesion and migration pathways.
EDIL3 (EGF-like repeats and discoidin I-like domains 3, also known as Del-1) is a secreted integrin ligand that binds to integrin ??v??3 and ??v??5 receptors, triggering the phosphorylation of focal adhesion kinase (FAK) and subsequent activation of downstream PI3K/Akt and ERK1/2 pathways. This signaling axis promotes endothelial cell survival, migration, and angiogenesis. EDIL3 also exerts anti-inflammatory effects by inhibiting nuclear factor-??B (NF-??B) transcriptional activity, thereby downregulating intercellular adhesion molecule 1 (ICAM-1) expression. Upstream regulators of EDIL3 include hypoxia-inducible factor 1?? (HIF-1??), vascular endothelial growth factor (VEGF), transforming growth factor ??1 (TGF-??1), and inflammatory cytokines such as tumor necrosis factor ?? (TNF-??) and interleukin-1?? (IL-1??). Key downstream targets include FAK, Src, Akt, ERK1/2, NF-??B, ICAM-1, Bcl-2, and matrix metalloproteinases MMP-2 and MMP-9. Additionally, EDIL3 interacts with phosphatidylserine, further modulating integrin-mediated signaling.
In HeLa cells, EDIL3 expression contributes to integrin-dependent adhesion, pro-survival signaling, and cytokine regulation. Knockout of EDIL3 in this background allows dissection of its role in cancer cell adhesion, resistance to anoikis, and cross-talk with inflammatory pathways. Given that HeLa cells harbor activated PI3K/Akt signaling due to HPV oncoproteins, this model provides a platform to study how EDIL3 loss influences tumor-relevant phenotypes such as anchorage-independent growth and matrix invasion.
Typical research applications include investigating EDIL3 function in angiogenesis and tumor progression using in vitro adhesion, scratch wound migration, and Matrigel invasion assays, as well as in vivo xenograft tumor growth studies. This knockout model is also suited for dissecting integrin-to-NF-??B signaling via luciferase reporter assays and flow cytometric quantification of ICAM-1 surface expression. Western blotting and RT-qPCR enable verification of EDIL3 depletion and monitoring of downstream targets such as FAK, Akt, and MMP-2. Co-immunoprecipitation experiments can assess the impact of EDIL3 loss on integrin ??v??3 complex formation. For additional application protocols or technical inquiries, please contact Ascent Research.
