The PCK1 antibody is a crucial tool for studying phosphoenolpyruvate carboxykinase 1 (PCK1), a rate-limiting enzyme in gluconeogenesis that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate. Expressed predominantly in the liver, kidneys, and adipose tissue, PCK1 plays a central role in glucose homeostasis, lipid metabolism, and insulin signaling. Its cytoplasmic isoform (PCK1) and mitochondrial counterpart (PCK2) are structurally distinct, with PCK1 being more directly linked to gluconeogenesis. Dysregulation of PCK1 is associated with metabolic disorders, including type 2 diabetes, obesity, and non-alcoholic fatty liver disease (NAFLD). Additionally, emerging research highlights its involvement in cancer progression, as some tumors exploit PCK1 to support anabolic growth under nutrient stress.
The PCK1 antibody enables researchers to detect and quantify PCK1 protein levels in various biological samples using techniques like Western blotting, immunohistochemistry, and immunofluorescence. It aids in exploring tissue-specific expression patterns, regulatory mechanisms (e.g., hormonal control by insulin or glucocorticoids), and interactions with metabolic pathways. Commercial PCK1 antibodies are typically validated for specificity against recombinant proteins or knockout models to minimize cross-reactivity. However, users must verify experimental conditions, as PCK1 expression can vary with nutritional status, circadian rhythms, or disease states. This antibody remains pivotal for advancing studies on metabolic diseases, cancer metabolism, and therapeutic targeting of gluconeogenesis.