Enolases have been characterized as highly conserved cytoplasmic glycolytic enzymes that may be involved in differentiation. Three isoenzymes have been identified, ? Enolase, ? Enolase and ? Enolase. ? Enolase expression has been detected on most tissues, whereas ? Enolase is expressed predominantly in muscle tissue and ? Enolase is detected only in nervous tissue. These isoforms exist as both homodimers and heterodimers, and they play a role in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway.
Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the human NSE protein and mouse myeloma Ag8563 cells. Sequence common in human, mouse and chicken.
Serum, brain, pancreas, liver, skeletal muscle and endocrine tumors. Expression stronger in tumor versus normal tissue.
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Left and Center: Immunohistochemical staining of normal pancreas tissue (left) and small bowel tumor tissue (center) using NSE antibody (X2070M and X2071M).Right: Western blot analysis using NSE antibodies (X2070M and X2071M) on ? and ? enolase standards.
1. Kang, J.L., et al. (1996). Immunoreactive neuron-specific enolase (NSE) is expressed in testicular carcinoma-in-situ. J. Pathol. 178(2):161-165.2. Koch, M., et al. (2007). Plasma S100beta and NSE levels and progression in multiple sclerosis. J. Neurol. Sci. 252(2):154-158.3. Oertel, M., et al. (2006). S-100B and NSE: markers of initial impact of subarachnoid haemorrhage and their relation to vasospasm and outcome. J. Clin. Neurosci. 13(8):834-840.