-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, -enolase is primarily localized to the cytoplasm, however, an alternatively translated form localizes to the nucleus and lacks glycolytic enzyme activity.1,2 -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 -enolase to facilitate aerobic glycolysis and contribute to the Warburg effect in tumor cells.2 -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 -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.5,6,7,8Technical InformationSynonymsEnolase-1Purity95% estimated by SDS-PAGESourceRecombinant enolase purified from E. coliAmino Acids1-434 (full length)MW47.74 kDaFormulation20 mM HEPES, pH 7.5, 150 mM sodium chloride, and 5% glycerolUniProt Accession P06733