Research Papers:

Characterization of the Human Folate Receptor Alpha Via Novel Antibody-Based Probes

Daniel J. O’Shannessy _, Elizabeth B. Somers, Earl Albone, Xin Cheng, Young Chul Park, Brian E. Tomkowicz, Yoshitomo Hamuro, Thomas O. Kohl, Tracy M. Forsyth, Robert Smale, Yao-Shi Fu and Nicholas C. Nicolaides

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Oncotarget. 2011; 2:1227-1243. https://doi.org/10.18632/oncotarget.412

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Daniel J. O’Shannessy1, Elizabeth B. Somers1, Earl Albone1, Xin Cheng1, Young Chul Park1, Brian E. Tomkowicz2, Yoshitomo Hamuro3, Thomas O. Kohl4, Tracy M. Forsyth4, Robert Smale5, Yao-Shi Fu5, Nicholas C. Nicolaides1

1 Morphotek Inc., 210 Welsh Pool Road, Exton, PA 19342, USA

2 Centocor Inc. Malvern, PA, USA

3 ExSAR Corporation, Monmouth Junction, NJ, USA

4 Rockland Immunochemicals, Inc., Gilbertsville, PA, USA

5 Laboratory Corporation of America, Los Angeles, CA, USA

Received: December 15, 2011; Accepted: December 27, 2011; Published: December 27, 2011;

Keywords: Folate receptor alpha, cancer, diagnostics, monoclonal antibody, protein structure, 26B3


Daniel J. O’Shannessy, email:


Folate receptor alpha (FRA) is a cell surface protein whose aberrant expression in malignant cells has resulted in its pursuit as a therapeutic target and marker for diagnosis of cancer. The development of immune-based reagents that can reproducibly detect FRA from patient tissue processed by varying methods has been difficult due to the complex post-translational structure of the protein whereby most reagents developed to date are highly structure-sensitive and have resulted in equivocal expression results across independent studies. The aim of the present study was to generate novel monoclonal antibodies (mAbs) using modified full length FRA protein as immunogen in order to develop a panel of mAbs to various, non-overlapping epitopes that may serve as diagnostic reagents able to robustly detect FRA-positive disease. Here we report the development of a panel of FRA-specific mAbs that are able to specifically detect FRA using an array of diagnostic platforms and methods. In addition, the methods used to develop these mAbs and their diverse binding properties provide additional information on the three dimensional structure of FRA in its native cell surface configuration.

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