α-Enolase Polyclonal Antibody

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 Cayman's α-Enolase Polyclonal Antibody can be used for Western blot and ELISA applications. The antibody recognizes α-enolase at ~47 kDa from human samples.

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).