Abstract
In the present paper, we describe a novel approach to map monoclonal antibody epitopes, using three new monoclonal antibodies that recognize h-TG2 (human transglutaminase 2) as an example. The target gene was fragmented and cloned upstream of an antibiotic-resistance gene, in the vector pPAO2, to select for in-frame polypeptides. After removal of the antibiotic-resistance gene by Cre/Lox recombination, an antigen fragment phage display library was created and selected against specific monoclonal antibodies. Using the h-TG2 fragment library, we were able to identify epitopes. This technique can also be broadly applied to the study of protein-protein interactions.
Original language | English |
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Pages (from-to) | 889-894 |
Number of pages | 6 |
Journal | Biochemical Journal |
Volume | 388 |
Issue number | 3 |
DOIs | |
Publication status | Published - 15 Jun 2005 |
Externally published | Yes |
Keywords
- Epitope mapping
- Phage display
- Transglutaminase
- β-lactamase