α-Enolase, also known as enolase 1, is a glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate.1 It is ubiquitously expressed in human tissues, including liver, spleen, kidney, and brain. In cells, α-enolase is primarily localized to the cytoplasm, however, an alternatively translated form localizes to the nucleus and lacks glycolytic enzyme activity.1,2 α-Enolase also functions as a cell surface receptor for plasminogen on pathogens and activated immune cells, as an oxidative stress protein in endothelial cells, and as a chromatin binding partner to facilitate transcription.2,3,4 The ENO1 promoter contains a hypoxia-response element, allowing α-enolase to facilitate aerobic glycolysis and contribute to the Warburg effect in tumor cells.2 α-Enolase is overexpressed in multiple tumors, including glioma, neuroblastoma, pancreatic, prostate, and hepatocellular carcinomas. Its role as a plasminogen receptor facilitates extracellular matrix degradation and cancer invasion.4 α-Enolase is an autoantigen in asthma, Hashimoto's encephalopathy, and rheumatoid arthritis, and has been found in the serum of pediatric patients with juvenile idiopathic arthritis.5,6,7,8 Cayman's α-Enolase Polyclonal Antibody can be used for Western blot and ELISA applications. The antibody recognizes α-enolase at ~47 kDa from human samples.WARNING This product is not for human or veterinary use.
