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Monoclonal antibody UJ 127:11 detects a 220,000‐240,000 kdal. Glycoprotein present on a sub‐set of neuroectodermally derived cells
Author(s) -
Kemshead J. T.,
Fritschy J.,
Garson J. A.,
Allan P.,
Coakham H.,
Brown S.,
Asser U.
Publication year - 1983
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910310209
Subject(s) - monoclonal antibody , microbiology and biotechnology , biology , antigen , antibody , glycoprotein , monoclonal , immunofluorescence , cell culture , immunology , genetics
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.