The ALDOC Knockout HeLa Polyclonal Cells are a CRISPR/Cas9-edited population of HeLa cells harboring targeted disruptions in the ALDOC gene. This heterogeneous polyclonal pool captures diverse gene-editing outcomes, avoiding clonal biases and enabling robust analysis of ALDOC loss-of-function phenotypes. These cells serve as a versatile model for studying aldolase C-dependent metabolic and signaling processes in a well-established cancer cell background.
The HeLa host cell line, derived from a cervical adenocarcinoma, is an immortalized epithelial model extensively used in metabolic and cancer research. HeLa cells exhibit rapid proliferation, rely heavily on aerobic glycolysis (the Warburg effect), and carry HPV-18 and p53 alterations. This background is ideal for investigating how ALDOC disruption alters glycolytic flux and tumor cell bioenergetics.
ALDOC encodes aldolase C, which catalyzes the reversible cleavage of fructose-1,6-bisphosphate into glyceraldehyde-3-phosphate and dihydroxyacetone phosphate, a pivotal step in glycolysis and gluconeogenesis. Aldolase C is regulated by HIF-1??, insulin, glucocorticoids, and c-Myc, and interacts with actin, tubulin, V-ATPase, phospholipase D, and ??-enolase, implicating it in metabolite channeling and cytoskeletal organization. ALDOC functions centrally in glycolysis/gluconeogenesis and fructose and mannose metabolism, linking carbon metabolism to the generation of ATP, pyruvate, and biosynthetic precursors. Consequently, ALDOC disruption attenuates glycolytic flux and shifts the balance between energy production and anabolic metabolism.
In HeLa cells, which exhibit a pronounced Warburg effect, ALDOC knockout impairs glycolytic capacity, reducing lactate secretion and dampening HIF-1??-mediated hypoxia responses. The loss of aldolase C may increase sensitivity to glycolytic inhibitors and nutrient deprivation. The polyclonal format permits analysis of metabolic plasticity and compensatory roles of other aldolase isoforms, providing a robust system for investigating aldolase C-specific contributions to proliferation, survival under stress, and the rationale for targeting glycolytic enzymes in cervical adenocarcinoma and other malignancies.
These cells support a broad range of functional assays, including Western blotting and RT-qPCR for confirming ALDOC knockdown, Seahorse glycolysis stress tests to measure glycolytic function, lactate production assays, cell viability assays under normoxic and hypoxic conditions, and immunofluorescence microscopy for assessing protein localization. The product is suitable for cancer metabolism research, glycolytic dependency studies, hypoxia adaptation investigations, and drug target validation. For additional technical information, please contact Ascent Research.
