The IGSF8 Knockout TE1 Polyclonal Cells constitute a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human TE1 esophageal epithelial cell line. This product provides a heterogeneous pool of cells carrying targeted disruptions at the IGSF8 locus, enabling robust loss-of-function analysis without the constraints of single-cell cloning. The polyclonal format preserves genetic diversity while ensuring consistent depletion of IGSF8 protein, making it a versatile tool for studying gene function in a cancer-relevant background. Researchers can employ this model to dissect IGSF8-dependent phenotypes in tetraspanin biology, growth factor signaling, and tumor cell migration.
The TE1 host cell line originates from a poorly differentiated human esophageal squamous cell carcinoma (ESCC). It retains hallmark oncogenic features of ESCC, including dysregulated proliferation and invasive potential, and expresses key tetraspanin and adhesion molecules. TE1 cells are widely used to model ESCC progression, metastatic dissemination, and response to environmental cues. Their epithelial origin and maintenance of relevant signaling networks make them an appropriate platform for interrogating the role of IGSF8 in cell motility and receptor tyrosine kinase modulation.
IGSF8, also known as EWI-2, is an immunoglobulin superfamily member that partitions into tetraspanin-enriched microdomains through direct interactions with CD81 and CD9. In these membrane platforms, IGSF8 functions as a negative regulator of platelet-derived growth factor receptor (PDGFR) and epidermal growth factor receptor (EGFR) signaling. Upon ligand stimulation, the CD81?CIGSF8 complex restrains receptor activation, leading to attenuated phosphorylation of ERK1/2 and AKT. This signaling brake subsequently reduces focal adhesion kinase (FAK) activity and downregulates matrix metalloproteinases MMP2 and MMP9, thereby suppressing cell migration and invasion. Upstream, IGSF8 function is influenced by integrin-mediated adhesion to extracellular matrix components, linking tetraspanin web organization to mechanotransduction.
In the TE1 esophageal carcinoma context, IGSF8 loss releases the inhibitory constraint on PDGFR and EGFR pathways, potentiating ERK/AKT activation and promoting a migratory, invasive phenotype. This polyclonal knockout model thus recapitulates a condition relevant to ESCC metastasis, where IGSF8 downregulation is frequently observed. The cells facilitate investigation of how IGSF8 orchestrates tetraspanin web assembly, receptor crosstalk, and integrin signaling in a disease-relevant setting. Researchers can compare wild-type TE1 responses with the knockout population to delineate IGSF8??s contribution to growth factor-driven cytoskeletal remodeling and tissue invasion.
This product is suited for a wide range of functional and mechanistic studies. Wound healing and transwell migration assays quantify IGSF8-dependent motility changes. PDGF or EGF stimulation combined with phospho-specific flow cytometry or Western blotting reveals altered ERK1/2 and AKT activation dynamics. Immunoprecipitation of CD81 or CD9 co-precipitates IGSF8, allowing confirmation of complex disruption, while RT-qPCR monitors transcriptional changes in MMP2 and FAK. Cell adhesion assays to extracellular matrix proteins assess integrin-mediated binding. For further information or technical support, please contact Ascent Research.
