Reconstitute with 0.2 mL of distilled water to yield a concentration of 500 µg/mL.
USP7 or HAUSP is a ubiquitin specific protease or a deubiquitylating enzyme that cleaves ubiquitin from its substrates. Since ubiquitylation (polyubiquitination) is most commonly associated with the stability and degradation of cellular proteins, HAUSP activity generally stabilizes its substrate proteins. HAUSP is most popularly known as a direct antagonist of Mdm2, the E3 ubiquitin ligase for the tumor suppressor protein, p53. Normally, p53 levels are kept low in part due to Mdm2-mediated ubiquitylation and degradation of p53. Interestingly, in response to oncogenic insults, HAUSP can deubiquitinate p53 and protect p53 from Mdm2-mediated degradation, indicating that it may possess a tumor suppressor function for the immediate stabilization of p53 in response to stress. Another important role of HAUSP function involves the oncogenic stabilization of p53. Oncogenes such as Myc and E1A are thought to activate p53 through a p19 alternative reading frame (p19ARF, also called ARF)-dependent pathway, although some evidence suggests ARF is not essential in this process. An intriguing possibility is that HAUSP provides an alternative pathway for safeguarding the cell against oncogenic insults.
蛋白别名: Deubiquitinating enzyme 7; Herpes virus-associated ubiquitin-specific protease; herpes-virus-associated ubiquitin-specific protease; Herpesvirus-associated ubiquitin-specific protease; mHAUSP; rHAUSP; Ubiquitin carboxyl-terminal hydrolase 7; ubiquitin specific protease 7; ubiquitin specific protease 7 (herpes virus-associated); Ubiquitin thioesterase 7; ubiquitin thiolesterase 7; Ubiquitin-specific-processing protease 7
基因别名: 2210010O09Rik; AA409944; AA617399; AU019296; AW548146; C80752; HAUSP; TEF1; USP7
分子生物学功能: cysteine protease