Cayman α-Enolase (human, recombinant)

α-Enolase, also known as enolase-1, is a glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. 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.^, 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.^,, The ENO1 promoter contains a hypoxia-response element, allowing α-enolase to facilitate aerobic glycolysis and contribute to the Warburg effect in tumor cells. 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. α-Enolase is an autoantigen in asthma, Hashimotos encephalopathy, and rheumatoid arthritis, and has been found in the serum of pediatric patients with juvenile idiopathic arthritis.^,,,

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