-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 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 It 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 -Enolase is also subject to citrullination by peptidyl arginine deiminases (PADs) and citrullinated -enolase has been found in the synovial fluid of rheumatoid arthritis patients.7Technical InformationSynonymsEnolase-1Purity90% estimated by SDS-PAGESourceRecombinant enolase purified from E. coli citrullinated by PAD4Amino Acids441MW47.74 kDaFormulationTBS, pH 7.4UniProt Accession P06733