一般描述
Human USP8 (Ubiquitin-Specific Protease 8) or UBPY, amino-acids 2-1118 (end) with an N-terminal FLAG-tag, expressed in a baculovirus-infected Sf9 cell expression system.
应用
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
生化/生理作用
Expression of ubiquitin-specific protease 8 (USP8) in mice is critical for proper expression and stability of several growth factor receptors including epidermal growth factor receptor. However, USP8 was shown to degrade chemokine receptor 4.
外形
Solution in 45 mM Tris-HCl, 124 mM NaCl, 2.4 mM KCl, 90 ng/μl Flag peptide, 3 mM DTT, and 20% Glycerol at pH 8.0.
储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
此项目有
Essential Role of Ubiquitin-Specific Protease 8 for Receptor Tyrosine Kinase Stability and Endocytic Trafficking In Vivo
Niendorf, S., et al.
Molecular and Cellular Biology, 727, 5029-5039 (2007)
The Deubiquitinating Enzyme USP8 Promotes Trafficking and Degradation of the Chemokine Receptor 4 at the Sorting Endosome
Berlin, I.
The Journal of Biological Chemistry, 285, 37895?37908-37895?37908 (2006)
Emi Mizuno et al.
Molecular biology of the cell, 16(11), 5163-5174 (2005-08-27)
Ligand-activated receptor tyrosine kinases undergo endocytosis and are transported via endosomes to lysosomes for degradation. This "receptor down-regulation" process is crucial to terminate the cell proliferation signals produced by activated receptors. During the process, ubiquitination of the receptors serves as
Sandra Niendorf et al.
Molecular and cellular biology, 27(13), 5029-5039 (2007-04-25)
Posttranslational modification by ubiquitin controls multiple cellular functions and is counteracted by the activities of deubiquitinating enzymes. UBPy (USP8) is a growth-regulated ubiquitin isopeptidase that interacts with the HRS-STAM complex. Using Cre-loxP-mediated gene targeting in mice, we show that lack
S Naviglio et al.
The EMBO journal, 17(12), 3241-3250 (1998-06-17)
The ubiquitin pathway has been implicated in the regulation of the abundance of proteins that control cell growth and proliferation. We have identified and characterized a novel human ubiquitin isopeptidase, UBPY, which both as a recombinant protein and upon immunoprecipitation
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