The CCDC127 Knockout HGC-27 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the HGC-27 human gastric carcinoma cell line, designed for targeted disruption of the CCDC127 gene. CCDC127 encodes a coiled-coil domain-containing protein with predicted involvement in centrosome function and primary cilium assembly. This polyclonal population encompasses a heterogeneous mix of cells carrying knockout alleles generated through CRISPR/Cas9-mediated gene disruption, providing a robust loss-of-function model without clonal selection artifacts. The product is suitable for researchers seeking to investigate the functional consequences of CCDC127 ablation in a cancer-relevant epithelial context, leveraging the inherent complexity of a non-clonal knockout background to capture population-level phenotypic variability.
The HGC-27 host cell line originates from a metastatic lymph node of a patient with undifferentiated gastric carcinoma, representing a well-established model of aggressive, metastatic gastric cancer. These epithelial cells retain key characteristics of their tumor origin, including a poorly differentiated phenotype and metastatic potential, making them a valuable system for studying tumor progression, invasion, and aberrant signaling. HGC-27 cells are widely employed in cancer biology to dissect molecular mechanisms driving gastric carcinogenesis and to evaluate therapeutic targets. The undifferentiated state of HGC-27 provides a relevant backdrop for examining how loss of CCDC127, a protein linked to primary cilium dynamics, may intersect with oncogenic pathways in a gastric cancer setting.
At the molecular level, CCDC127 is predicted to function in centrosome maintenance and primary cilium assembly, interacting with key centrosomal and ciliary proteins such as members of the CEP family and PCM1. Its role is closely tied to ciliogenesis and the Hedgehog signaling pathway, where it may influence the localization and activity of pathway components including IFT88, ARL13B, BBS proteins, the negative regulator SUFU, and downstream GLI transcription factors. Although specific upstream regulators remain uncharacterized, CCDC127 is thought to be cell cycle-regulated. Disruption of CCDC127 likely impinges on primary cilium formation and centrosome-related processes, thereby modulating Hedgehog signal transduction??a pathway critical for cell proliferation and differentiation. The precise mechanistic interplay between CCDC127 and these factors remains an active area of investigation, positioning this knockout tool as a key resource for elucidating these relationships.
In the context of HGC-27 gastric carcinoma cells, knockout of CCDC127 offers a powerful model to explore how centrosomal and ciliary protein dysfunction contributes to the malignant phenotype. Primary cilia are often dysregulated in cancer, and their role in Hedgehog signaling can influence tumor growth and metastasis. By disrupting CCDC127 in this undifferentiated, metastatic cell line, researchers can probe effects on cell cycle progression, migratory capacity, and colony formation, potentially linking centrosomal abnormalities to gastric cancer aggressiveness. The polyclonal format provides a realistic spectrum of knockout efficiencies, facilitating the study of how partial or complete loss of CCDC127 impacts cellular behavior in a heterogeneous population, which may mimic tumor heterogeneity.
This polyclonal knockout cell product is ideally suited for a range of applications, including ciliogenesis research, investigation of centrosomal proteins in cancer, and detailed signaling pathway analysis. Researchers can employ Western blotting and RT-qPCR to confirm protein and transcript level changes, immunofluorescence for ciliary markers such as acetylated tubulin and ARL13B to visualize primary cilia, flow cytometry for cell cycle profiling, and functional assays like migration and colony formation assays to assess metastatic traits. The model enables dissection of CCDC127 interactions with the Hedgehog machinery and centrosomal complexes, making it a valuable addition to cancer biology and cell signaling studies. For further details or custom modifications, please contact Ascent Research.
