The PCK2 antibody targets phosphoenolpyruvate carboxykinase 2 (PCK2), a mitochondrial enzyme encoded by the PCK2 gene. PCK2 catalyzes the conversion of oxaloacetate to phosphoenolpyruvate (PEP), a rate-limiting step in gluconeogenesis and a critical node connecting the tricarboxylic acid (TCA) cycle with glucose metabolism. Unlike its cytosolic isoform PCK1. PCK2 is primarily involved in cataplerosis, replenishing TCA intermediates and regulating energy homeostasis under nutrient-deprived conditions. It plays a role in insulin secretion, amino acid metabolism, and lipid synthesis, linking mitochondrial function to cellular metabolic flexibility.
PCK2 is upregulated in various cancers, where it supports tumor growth by fueling biosynthetic pathways and mitigating oxidative stress. Its expression is regulated by hormones (e.g., glucocorticoids), dietary states, and hypoxia-inducible factors. The PCK2 antibody is widely used to study tissue-specific expression, subcellular localization, and dynamic regulation of PCK2 in metabolic disorders (e.g., diabetes, NAFLD) and cancer. Applications include Western blotting, immunohistochemistry, and immunofluorescence to explore PCK2's role in metabolic reprogramming, mitochondrial bioenergetics, and therapeutic targeting. Research using PCK2 antibodies has highlighted its dual role in both physiological adaptation and pathological processes, making it a biomarker of interest in metabolic and oncological studies.