一般說明
Human USP14 (Ubiquitin-Specific Protease 14) or TGT (tRNA-guanine transglycosylase), amino acids 2-494 (end) with an N-terminal FLAG-tag, expressed in a baculovirus-infected Sf9 cell expression system.
Ubiquitin-Specific Protease 14 is a deubiquitinating protein responsible for the removal of ubquitin tags attached to proteins by α•NH-peptide bonds and the ε-NH-isopeptide bond.
Ubiquitin-Specific Protease 14 is a deubiquitinating protein responsible for the removal of ubquitin tags attached to proteins by α•NH-peptide bonds and the ε-NH-isopeptide bond.
USP14 has been shown to be phosphorylated by AKT which is required for protein stability and nuclear localization.
應用
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
外觀
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.
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
Nature cell biology, 14(7), 717-726 (2012-06-19)
The stability and membrane localization of the transforming growth factor-β (TGF-β) type I receptor (TβRI) determines the levels of TGF-β signalling. TβRI is targeted for ubiquitylation-mediated degradation by the SMAD7-SMURF2 complex. Here we performed a genome-wide gain-of-function screen and identified
Biochemical and biophysical research communications, 379(4), 995-1000 (2009-01-13)
Accumulation of unfolded proteins within the endoplasmic reticulum (ER) lumen induces ER stress. Eukaryotic cells possess the ER quality control systems, the unfolded protein response (UPR), to adapt to ER stress. IRE1alpha is one of the ER stress receptors and
RNA (New York, N.Y.), 16(5), 958-968 (2010-04-01)
The eukaryotic tRNA-guanine transglycosylase (TGT) has been reported to exist as a heterodimer, in contrast to the homodimeric eubacterial TGT. While ubiquitin-specific protease 14 (USP14) has been proposed to act as a regulatory subunit of the eukaryotic TGT, the mouse
The Journal of neuroscience : the official journal of the Society for Neuroscience, 29(35), 10909-10919 (2009-09-04)
Dysfunction of the ubiquitin proteasome system (UPS) has been implicated in the pathogenesis of many neurological diseases, including Alzheimer's, spinocerebellar ataxia, and several motor neuron diseases. Recent research indicates that changes in synaptic transmission may play a critical role in
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