alpha-Enolase (human, recombinant)

alpha-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, alpha-enolase is primarily localized to the cytoplasm, however, an alternatively translated form localizes to the nucleus and lacks glycolytic enzyme activity. alpha-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 alpha-enolase to facilitate aerobic glycolysis and contribute to the Warburg effect in tumor cells. alpha-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. alpha-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.Synonyms: Enolase-1. Purity: >95% estimated by SDS-PAGE. Protein Identity Confirmed by Mass Spec: Yes. Source: Recombinant enolase expressed in E. coli. Amino Acids: 1-434 (full length). MW: 47.74 kDa. Formulation: (Request formulation change), 20 mM HEPES, pH 7.5, 150 mM sodium chloride, and 5% glycerol. UniProt Accession #: P06733.