Monoclonal antibodies against the nonmucin domain of MUC1/episialin.
We have tested the reactivity of the monoclonal antibodies submitted to the ISOBM TD-4 Workshop for reactivity with a hybrid molecule consisting of the bacterial beta-galactosidase and most of the extracellular nonrepeat domain of MUC1/episialin. Two monoclonal antibodies submitted to the Workshop, 232A1 and M29, were directed against the protein moiety of this domain as shown by immunoblotting and immunoprecipitation.
Hilkens
J
J
Division of Tumor Biology, The Netherlands Cancer Institute (Antoni van Leeuwenhoekhuis), Amsterdam, The Netherlands. jhi@nnki.nl
Boer
M
M
D000911:Antibodies, Monoclonal / Q000032:analysis*; D000918:Antibody Specificity / Q000276:immunology; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D015151:Immunoblotting; D018396:Mucin-1 / Q000276:immunology*; D009363:Neoplasm Proteins / Q000235:genetics / Q000276:immunology*; D011233:Precipitin Tests; D011993:Recombinant Fusion Proteins; D014162:Transfection; D001616:beta-Galactosidase / Q000235:genetics / Q000276:immunology
D000911:Antibodies, Monoclonal; D018396:Mucin-1; D009363:Neoplasm Proteins; D011993:Recombinant Fusion Proteins; D001616:beta-Galactosidase