Recombinant Human ZRANB1, His-tagged ZRANB1-158H

Recombinant Human ZRANB1, His-tagged

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Recombinant Human ZRANB1, His-tagged

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Cat.No. : ZRANB1-158H
Product Overview : Recombinant human ZRANB1 (amino acid residues 245-697), fused with N-terminal His, was expressed in E. coli.
Description : TRABID is a cysteine protease and is a member of the OTU (ovarian tumour) superfamily of proteins (Balakirev et al., 2003). Cloning of the human gene was first described by Evans et al. (1992). TRABID was recently reported to specifically and positively regulate the Wnt signalling pathway. TRABID is composed of a tumour necrosis factor receptor associated factor (TRAF) binding domain in the C-terminus and three Zinc-finger (ZnF) motifs at the N-terminus.
Source : E. coli
Species : Human
Tag : His
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-TRABID CD(245-697) was validated by the monitoring of mono-ubiquitin generation as a result of the enzyme catalysed cleavage of K63-linked di-ubiquitin. Incubation of the substrate in the presence or absence of His-TRABID CD(245-697) was compared confirming the deubiquitylating activity of His-TRABID CD(245-697).
Molecular Mass : ~54.8kDa
Purity : >81% by SDS-PAGE
Storage : 12 months at -70°C. Avoid multiple freeze/thaw cycles.
Concentration : 0.5 mg/ml
Gene Name : ZRANB1 zinc finger, RAN-binding domain containing 1 [ Homo sapiens ]
Official Symbol : ZRANB1
Synonyms : ZRANB1; zinc finger, RAN-binding domain containing 1; ubiquitin thioesterase ZRANB1; TRABID; hTrabid; TRAF-binding protein domain; TRAF-binding domain-containing protein; zinc finger Ran-binding domain-containing protein 1; DKFZp762P2216;
Gene ID : 54764
mRNA Refseq : NM_017580
Protein Refseq : NP_060050
MIM : 611749
UniProt ID : Q9UGI0
Chromosome Location : 10q26.12
Function : K63-linked polyubiquitin binding; cysteine-type peptidase activity; metal ion binding; peptidase activity; protein binding; ubiquitin thiolesterase activity; ubiquitin-specific protease activity; zinc ion binding;

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