p53 Monoclonal Antibobies

Monoclonal antibodies (mAbs) directed against the p53 protein have been invaluable tools for both clinical and basic research.
In clinical laboratories, the use of various p53 mAbs has led to an extensive series of immunohistochemical analyses for the rapid identification of p53 alteration (Dowell et al., 1994).
In the area of basic research research, these mAbs have permitted detailed studies of the various conformations of the p53 protein ( Milner; Gannon and Legros).

The production of several panels of mAbs directed against human p53 has led to the various observations.

• Firstly , p53 is clearly a highly immunogenic protein.
• Secondly , more than 95% of the various mAbs recognize epitopes which are localized in the amino, or (to a lesser extent) in the carboxy, terminus of the protein ( Legros and Bartek). The only way to obtain mAbs towards the central region of the p53 protein is through the immunization of mice with a truncated form of p53, lacking both extremities ( Legros and Vojtesek).
• Thirdly , out of over 100 anti-p53 mAbs described in the literature, only two (PAb1620 and PAb246) recognize non-sequential epitopes, which have not yet been mapped. The binding sites of all the other mAbs were identified by the use of phage-displayed peptide libraries or recombinant fragments of p53 protein or by Pepscan analysis ( Legros; Wade; Stephen and Stephen).

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