The GOLGA5 Knockout SK-HEP-1 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal knockout cell population derived from the human hepatic adenocarcinoma line SK-HEP-1. This product provides a loss-of-function model for studying the Golgin subfamily A member 5 (GOLGA5) protein, essential for Golgi stack maintenance and vesicle tethering. The polyclonal pool ensures a heterogeneous genetic background suitable for functional assays where clonal uniformity is not required.
SK-HEP-1 cells originate from ascites fluid of a patient with liver adenocarcinoma, serving as a well-characterized model for hepatic tumor biology. They exhibit epithelial morphology and retain malignant features such as proliferative capacity and invasiveness. This host line provides a pathologically relevant context for interrogating the role of Golgi organization in cancer cell phenotypes.
GOLGA5, a transmembrane golgin, is integral to maintaining Golgi ribbon structure and directing intra-Golgi vesicle traffic. It interacts with GM130 and giantin to anchor vesicles, and its function depends on small GTPases ARF1 and Rab1. COPI and COPII coat complexes, along with SNAREs, coordinate with GOLGA5-mediated tethering to ensure proper protein trafficking, glycosylation, and secretion. Disruption of GOLGA5 leads to Golgi fragmentation, mislocalization of Golgi enzymes, and altered secretory cargo transport, thereby impairing downstream cellular processes.
In liver cancer cells, GOLGA5 knockout enables investigation of how Golgi disorganization affects tumor-associated processes. Aberrant Golgi morphology in cancers is linked to altered glycosylation and secretion of factors that modulate tumor microenvironment and signaling. This model allows researchers to examine whether Golgi integrity is required for SK-HEP-1 migration, invasion, and receptor presentation, linking secretory dysfunction to oncogenic behavior.
Researchers can employ these cells in immunofluorescence and Golgi imaging to visualize structure, secretion assays to measure trafficking efficiency, and western blotting to detect glycosylation changes. Migration and invasion assays further reveal the contribution of GOLGA5 to metastatic potential. The model is also suited for evaluating Golgi-targeted drug delivery systems. For detailed product information, custom inquiries, or technical support, please contact Ascent Research.
