This product is a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human colorectal adenocarcinoma cell line HT29, featuring targeted disruption of the ANTXR2 gene (also known as CMG2). The polyclonal format provides a heterogeneous pool of edited cells, enabling robust loss-of-function studies without selection bias from single-cell cloning.
HT29 cells originate from a human colorectal adenocarcinoma and are extensively employed as an intestinal epithelial model for studying colorectal cancer pathogenesis, epithelial barrier function, and cell-matrix interactions. Their adherent growth and well-characterized signaling networks make them particularly suitable for investigating genes involved in adhesion and integrin-mediated pathways.
ANTXR2 (CMG2) is a transmembrane receptor that binds to collagen IV, laminin, and anthrax protective antigen, thereby mediating cell adhesion to the extracellular matrix and internalization of anthrax toxin. Its activation by ECM ligands triggers recruitment of talin and vinculin to nascent adhesions and engages integrins, notably ITGB1, leading to FAK and SRC phosphorylation. This initiates downstream signaling cascades including Rho GTPase-mediated cytoskeletal reorganization, cell spreading, and MAPK/ERK pathway activation. Additionally, ANTXR2 participates in endocytic trafficking of anthrax toxin via clathrin-dependent mechanisms. By disrupting ANTXR2, the cells lose a key nexus for ECM-integrin cross-talk, likely impairing focal adhesion dynamics and attenuating signals transmitted through FAK-SRC-Rho GTPase and MAPK/ERK modules.
Within the HT29 colorectal adenocarcinoma background, ANTXR2 knockout is predicted to markedly reduce cellular attachment to collagen IV and laminin, alter focal adhesion turnover, and disrupt cytoskeletal organization driven by Rho family GTPases. These changes provide a valuable platform for dissecting ECM-dependent signaling in intestinal epithelial and colorectal cancer contexts, particularly the interplay between ANTXR2 and integrin-mediated pathways. Moreover, the loss of the anthrax protective antigen receptor renders the cells resistant to anthrax toxin, enabling precise dissection of toxin internalization pathways separate from endogenous receptor function. This model thus addresses both cancer cell biology and toxin susceptibility research.
A broad range of experimental applications is supported by this tool, including anthrax toxin resistance profiling, analysis of cell-ECM adhesion strength, colorectal cancer migration and invasion assays, and functional modeling of hyaline fibromatosis syndrome. Researchers can validate ANTXR2 disruption using western blotting, RT-qPCR, immunofluorescence, and flow cytometry. Functional studies may employ ECM adhesion assays with collagen IV or laminin substrates, anthrax toxin sensitivity tests, wound healing or transwell migration assays, and co-immunoprecipitation to assess protein interactions. For additional technical specifications and ordering information, please contact Ascent Research.
