Millipore Technical Publications |
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Use of Multiple Assay Platforms to Investigate the p53-MDM2 Interaction and its Influence on p53 Ubiquitination | ||
| Lit No: | PS3378EN00 | |
| Year: | 2012 | |
| Introduction Robust, scalable, and biologically-informative assays for ubiquitin processes have the potential to reveal new biology for therapeutic exploitation. Here, we demonstrate how such tools can be used to examine two distinct steps – E3-substrate binding and ubiquitin ligation – in the well studied MDM2-p53 system. p53 is expressed in a wide variety of tissues and plays a major role in preventing tumour development. It is involved in cell cycle regulation, functioning as a trans-activator to negatively regulate cell division by stimulating apoptosis or growth arrest. Defects in p53 expression have been implicated in several diseases including choroid plexus papilloma, lung cancer, head/neck squamous cell carcinomas, oesophageal squamous cell carcinoma, Li-Fraumeni syndrome, and hereditary adrenocortical carcinoma. Click the PDF above for the full document. | |
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