Species : |
Human |
Source : |
E.coli |
Tag : |
His |
Protein Length : |
1-202 a.a. |
Description : |
JOSD1 is a cysteine protease and a member of the Machado-Joseph Domain (MJD) enzyme family. Cloning of the human gene was first described by Nomura et al. (1994). The Josephin domain is a conserved cysteine protease domain found in four human deubiquitylating enzymes: ataxin-3, the ataxin-3-like protein (Ataxin-3L), Josephin-1 (JOSD1), and Josephin-2 (JOSD2). Two of the human Josephin proteins, ataxin-3 and ataxin-3L, each contain a single Josephin domain at their N-terminus plus a flexible C-terminal domain of comparable length. JOSD1 and JOSD2, on the other hand, are each composed solely of a single Josephin domain (Weeks et al., 2011). |
Form : |
50 mM HEPES pH 7.5, 150 mM sodium chloride, 2 mM dithiothreitol, 10% glycerol |
Bio-activity : |
Deubiquitylase Enzyme Assay: The activity of His-JOSD1 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 His-JOSD1 was compared confirming the deubiquitylating activity of His-JOSD1. |
Molecular Mass : |
~26 kDa |
Purity : |
>98% by SDS-PAGE |
Storage : |
12 months at -70°C. Avoid multiple freeze/thaw cycles. |
Concentration : |
0.5 mg/ml |