Monoclonal antibody UJ 127:11 detects a 220,000‐240,000 kdal. Glycoprotein present on a sub‐set of neuroectodermally derived cells

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Abstract
The monoclonal antibody UJ 127‐11 was raised following immunization of mice with human foetal brain and subsequent somatic cell hybridization of spleen cells with the mouse myeloma cell line P3‐X63‐Ag8‐653. Studies on normal foetal and adult tissues show that, by indirect immunofluorescence, the antigen recognized by UJ 127:11 is restricted in its expression to cells of neural rather than glial origin. Neural tumours such as neuroblastoma, medulloblastoma and ganglioglioma (neural component) bind the monoclonal antibody whereas malignancies originating from glial cells do not bind UJ 127:11. Biochemically the monoclonal antibody has been shown to bind to a glycoprotein of 220,000‐240,000 mol. wt. under reducing and non‐reducing conditions. Despite similarities in the molecular weight between human fibronectin and the antigen recognized by UJ 127:11, they have different serological and biochemical characteristics, suggesting that the monoclonal antibody is not binding to either cell or plasma fibronectin.

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