USP7 (Ubiquitin-specific-processing protease 7) is a deubiquitinase that has been shown to regulate the p53-Mdm2 pathway (1). Cotransfection of p53 and USP7 stabilizes p53 through the removal of ubiquitin moieties from polyubiquitinated p53 (1). It also counteracts the destabilizing effect of Mdm2 by direct deubiquitination of p53 (2). Subsequently, USP7 has been shown to deubiquitinate Mdm2 and Mdmx, thereby stabilizing these proteins (2). USP7 interacts with herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 and Epstein-Barr virus EBNA1. EBNA1 shows a tenfold higher affinity than TP53 and can compete with it for USP7 binding (3).
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