The GOLGA2 Knockout 769-P Polyclonal Cells constitute a CRISPR/Cas9-edited human polyclonal knockout cell population targeting the GOLGA2 gene. Generated in the 769-P host background without clonal isolation, this loss-of-function model provides a heterogeneous pool for studying gene disruption effects. Cells are supplied as a ready-to-use polyclonal population, enabling immediate functional genomics experiments without single-cell cloning bottlenecks.
The parental 769-P cell line is an epithelial adherent line derived from a human clear cell renal cell carcinoma (ccRCC). This well-characterized kidney cancer model retains hallmark mutations and signaling aberrations of ccRCC, making it a clinically relevant platform for investigating tumor biology, including cell growth, migration, and therapeutic responses in renal cell carcinoma.
GOLGA2 encodes GM130, a peripheral cis-Golgi matrix protein that orchestrates Golgi ribbon formation and vesicle tethering. Mechanistically, GM130 is phosphorylated by CDK1 and regulated by PLK1 during mitosis, driving Golgi disassembly. It directly interacts with USO1 (p115), GORASP1 (GRASP55), GORASP2 (GRASP60), STX5, and VAPA to facilitate cisternal stacking and post-mitotic Golgi reassembly. Downstream, GM130 influences RAB GTPase-mediated trafficking and participates in autophagosome biogenesis, linking Golgi organization to autophagy and mitotic spindle assembly.
In clear cell renal cell carcinoma, Golgi fragmentation and dysregulated secretion contribute to malignant phenotypes and drug resistance. Disrupting GOLGA2 in the 769-P model allows dissection of how GM130 loss impacts USO1-dependent tethering, GORASP-mediated stacking, and RAB-dependent trafficking within a cancer context. This system is valuable for examining the interplay between Golgi integrity, autophagy regulation, and mitotic fidelity in ccRCC, potentially unveiling vulnerabilities specific to renal tumors.
Researchers can employ the GOLGA2 Knockout 769-P Polyclonal Cells in diverse assays, including western blotting for protein depletion confirmation, immunofluorescence to assess Golgi morphology disruption, cell proliferation and cell cycle analyses to evaluate growth defects, wound healing assays to measure migration, and drug sensitivity screens to probe chemotherapeutic effects. These cells are adaptable for functional studies of Golgi-dependent cancer mechanisms. For further technical details or support, please contact Ascent Research.
