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一般說明
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.
應用
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.
外觀
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.
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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)
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
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
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)
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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