New Monoclonal Antibodies Recognizing p53 Protein Phosphorylated by Casein Kinase II at Serine 392
| Authors | |
|---|---|
| Year of publication | 2001 |
| Type | Article in Periodical |
| Magazine / Source | Folia Biologica |
| MU Faculty or unit | |
| Citation | |
| Field | Oncology and hematology |
| Description | The p53 tumour suppressor protein is a nuclear phosphoprotein which plays a key role in cell cycle regulation. One of the critical issues of p53 response to cellular stress or DNA damage is the way of its activation. It has been suggested that posttranslational modification involving phosphorylation of p53 protein is most likely the mechanism through which the activity of p53 protein may be regulated. Recently, it has been also shown that phosphorylation of Ser392 is important for p53-mediated transcriptional activation in vivo. Preparation of the monoclonal antibodies that are specific to either phosphorylated or unphosphorylated epitopes within the target protein provides a powerful technique for studying the role of p53. |
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