α-Enolase (human, recombinant)

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

WARNING This product is not for human or veterinary use.

1. Zhu, X., Miao, X., Wu, Y., et al. ENO1 promotes tumor proliferation and cell adhesion mediated drug resistance (CAM-DR) in non-Hodgkin’s lymphomas. Exp. Cell Res. 335(2), 216-223 (2015).

2. Song, Y., Luo, Q., Long, H., et al. Alpha-enolase as a potential cancer prognostic marker promotes cell growth, migration, and invasion in glioma. Mol. Cancer 13, 65 (2014).

3. Subramanian, A., and Miller, D.M. Structural analysis of α-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. The Journal of Biological Chemisty 275(8), 5958-5965 (2000).

4. Hsiao, K.-C., Shih, N.-Y., Fang, H.-L., et al. Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target. PLoS One 8(7), e69354 (2013).

5. Nahm, D.-H., Lee, K.-H., Shin, J.-Y., et al. Identification of α-enolase as an autoantigen associated with severe asthma. J. Allergy Clin. Immunol. 118(2), 376-381 (2006).

6. Moore, T.L., Gillian, B.E., Crespo-Pagnussat, S., et al. Measurement and evaluation of isotypes of anti-citrullinated fibrinogen and anti-citrullinated α-enolase antibodies in juvenile idiopathic arthritis. Clin. Exp. Rheumatol. 32(5), 740-746 (2014).

7. Yoneda, M., Fujii, A., Ito, A., et al. High prevalence of serum autoantibodies against the amino terminal of α-enolase in Hashimoto’s encephalopathy. J. Neuroimmunol. 185(1-2), 195-200 (2007).

8. Cong, Y., Wang, L., Peng, R., et al. Timosaponin AIII induces antiplatelet and antithrombotic activity via G_q-mediated signaling by the thromboxane A₂ receptor. Sci. Rep. 6, 38757 (2016).

Moon, J.-S., Younis, S., Ramadoss, N.S., et al. Cytotoxic CD8⁺ T cells target citrullinated antigens in rheumatoid arthritis. Nat. Commun. 14(1), 319 (2023).