U6260
Ubiquitin-Specific Protease 10 human
recombinant, expressed in Sf9 cells, ≥56% (SDS-PAGE)
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关于此项目
NACRES:
NA.54
UNSPSC Code:
12352204
Recombinant:
expressed in Sf9 cells
Concentration:
≥56% (SDS-PAGE)
General description
Human USP10 (Ubiquitin-Specific Protease 10) or Ubiquitin C-terminal Hydrolase 10, amino acids 2-798 (end) with an N-terminal FLAG-tag, expressed in a baculovirus-infected Sf9 cell expression system.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
Ubiquitin-specific protease 10 (USP10) expression has been shown to be induced by vasopressin. In HEK293 cells, USP10 was shown to deubiquitylate sorting nexin 3.
Physical form
Solution in 40 mM Tris-HCl, 110 mM NaCl, 2.2 mM KCl, 80 ng/μl Flag peptide, 3 mM DTT, and 20% Glycerol at pH 8.0.
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Hortensia Faus et al.
Molecular and cellular endocrinology, 245(1-2), 138-146 (2005-12-22)
The role of the ubiquitin/proteasome system in degrading nuclear hormone receptors and regulating their transcriptional function has emerged in the last few years. We identified the ubiquitin-specific protease USP10 as part of DNA-bound androgen receptor (AR) complexes purified from nuclear
Jian Yuan et al.
Cell, 140(3), 384-396 (2010-01-26)
Stability and localization of p53 is essential for its tumor suppressor function. Ubiquitination by the E3 ubiquitin ligase Mdm2 is the major regulatory mechanism of p53, which induces p53 nuclear export and degradation. However, it is unclear whether ubiquitinated cytoplasmic
Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3.
Boulkroun S.
American Journal of Physiology: Renal Physiology, 295, F889-F900 (2008)
C Soncini et al.
Oncogene, 20(29), 3869-3879 (2001-07-06)
Degradation of cellular proteins through ubiquitination is a fundamental strategy for regulating biological pathways. De-ubiquitination, i.e. the removal of ubiquitin from proteins and peptides to which ubiquitin is attached, is catalyzed by processing proteases known as de-ubiquitinating enzymes. We are
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