| Species : |
Human |
| Source : |
E.coli |
| Tag : |
GST |
| Protein Length : |
81-461 a.a. |
| Description : |
There are two main classes of DUB; cysteine proteases and metalloproteases. Ubiquitin specific protease 36 (USP36) is a member of the cysteine protease enzyme family and cloning of the human gene was first described by Nagase et al. (2000). USP36 is primarily localized to the nucleoli, is required to maintain normal nucleolar structure and is highly expressed in skeletal muscle and testis. Nucleophosmin and fibrillarin are two nucleolar proteins that have been shown to undergo ubiquitylation, and are substrates for USP36. The deubiquitylating activity of USP36 controls transcriptional regulation and ribosome biogenesis in response to the changes in environmental conditions (Endo et al., 2009). |
| Form : |
50 mM HEPES pH 7.5, 150 mM sodium chloride, 2 mM dithiothreitol, 10% glycerol |
| Bio-activity : |
Deubiquitylase Enzyme Assay: The activity of GST-USP36 was validated by determining the increase in fluorescence measured as a result of the enzyme catalysed cleavage of the fluorogenic substrate Ubiquitin-Rhodamine110-Glycine generating Ubiquitin and Rhodamine110-Glycine. Incubation of the substrate in the presence or absence of GST-USP36 was compared confirming the deubiquitylating activity of GST-USP36. |
| Molecular Mass : |
~69 kDa |
| Purity : |
>84% by SDS-PAGE |
| Storage : |
12 months at -70°C. Avoid multiple freeze/thaw cycles. |
| Concentration : |
0.5 mg/ml |