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Disease Markers
Volume 14 (1998), Issue 2, Pages 99-112

Monoclonal Antibody Recognizing a Core Epitope on Mucin

Peter L. Devine,1 Rachel J. Quin,1 Paul W. Shield,2 Yew Wah Liew,3 John K. Sheehan,4 and David J. Thornton4

1Department of Obstetrics and Gynaecology, The University of Queensland, Australia
2Division of Cytopathology, Pathology Department, Royal Brisbane Hospital, Queensland, Australia
3Red Cross Blood Transfusion Service, Australian Red Cross Society, Queensland, Australia
4Department of Biochemistry and Molecular Biology, University of Manchester, United Kingdom

Received 9 December 1999; Accepted 9 December 1999

Copyright © 1998 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Monoclonal antibody TH1 (IgM) was prepared by immunizing mice with deglycosylated (TFMSA-treated) cystic fibrosis mucin. TH1 reacted strongly with TFMSA treated cystic fibrosis mucin but not with the fully glycosylated mucin, indicating reactivity with a core mucin epitope. TH1 showed no reactivity with ovine mucin (98% of glycans as sialyl-Tn) but reacted strongly with desialylated ovine mucin, indicating the epitope for this mab was the Tn-antigen (O-linked GalNAc). However, TH1 showed no reactivity with Tn-positive red blood cells, and the binding of TH1 was not inhibited by GalNAc at 2.5 mg/ml, illustrating the importance of the peptide sequence to which the GalNAc is attached. TH1 stained the majority of cancers of the colon, lung, stomach, ovary, breast, and cervix, and the cellular distribution of this antigen in normal tissue suggested reactivity with immature mucin. This antibody appears to be a useful reagent for the detection of immature mucin.