The DPP9 Knockout HGC-27 Polyclonal Cells product provides a CRISPR/Cas9-mediated polyclonal knockout cell population in which the DPP9 gene has been disrupted within the HGC-27 human gastric adenocarcinoma cell line. This pooled knockout format preserves the natural genetic diversity of the edited cell pool, offering a robust and efficient model for functional genomics studies, pathway analysis, and loss-of-function screening without the need for single-cell cloning. The heterogeneous population is ideal for high-content assays, drug target validation, and investigations into DPP9-dependent signaling networks, enabling reproducible assessment of phenotypic outcomes while minimizing clonal artifacts.
HGC-27 is a poorly differentiated gastric adenocarcinoma cell line originally derived from a lymph node metastasis of a Japanese patient. This cell line recapitulates key features of metastatic gastric cancer, including rapid proliferation, anchorage-independent growth, and invasive capacity. As a widely accepted model for gastric cancer research, HGC-27 retains the molecular characteristics of advanced disease, making it particularly suitable for studying mechanisms governing tumor cell dissemination, epithelial-mesenchymal transition, and tumor?Cstroma interactions. The metastatic origin and aggressive phenotype of HGC-27 provide a clinically relevant background for dissecting the role of DPP9 in gastric cancer progression.
Dipeptidyl peptidase 9 (DPP9) is a serine protease that cleaves N-terminal dipeptides from peptide substrates containing proline or alanine at the penultimate position, thereby modulating the bioactivity of numerous signaling peptides. DPP9 expression and activity are regulated by upstream mediators including TGF-??, TNF-??, IL-1??, and EGF. Functionally, DPP9 forms intracellular complexes with the related protease DPP8 and the fibronectin leucine-rich transmembrane protein FLRT3, and through these interactions it negatively regulates the NLRP1 inflammasome. By suppressing NLRP1, DPP9 restrains downstream assembly of ASC and activation of caspase-1, thereby limiting proteolytic maturation and secretion of pro-inflammatory IL-1??. In parallel, DPP9-mediated processing influences levels of chemokines such as CXCL10 and neuropeptides including substance P, linking DPP9 activity to cell adhesion, migration, apoptosis, and immune signaling.
In the context of gastric cancer, DPP9 has been implicated in the control of cell adhesion, migration, and apoptotic pathways that are dysregulated during malignant progression. Disruption of DPP9 in the metastatic HGC-27 background allows researchers to investigate how loss of DPP9 function affects NLRP1 inflammasome activation and downstream inflammatory cascades, potentially altering the tumor microenvironment and immune cell recruitment. Moreover, DPP9 knockout may impact FLRT3-dependent cell adhesion and CXCL10-mediated chemotaxis, providing a platform to study the interplay between DPP9 and metastatic behavior. This polyclonal knockout model thus enables functional dissection of DPP9??s role in gastric cancer cell dissemination, apoptosis resistance, and immune evasion.
Typical applications of this product include gastric cancer biology research, NLRP1 inflammasome regulation studies, drug target validation, cell migration and invasion assays, and immune modulation experiments. The polyclonal knockout cells are compatible with a broad range of assays such as western blotting, RT-qPCR, colony formation, apoptosis assays, and NLRP1 inflammasome activation readouts including caspase-1 cleavage and IL-1?? ELISA. Co-immunoprecipitation can be employed to explore DPP9 protein interactions, while chemotaxis assays enable assessment of migratory behavior. Researchers seeking to utilize this advanced cell model for their studies are encouraged to contact Ascent Research for further technical details and customization options.
