U6385
Ubiquitin-Specific Protease 14 human
recombinant, expressed in Sf9 cells, ≥75% (SDS-PAGE)
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NACRES:
NA.54
UNSPSC Code:
12352204
Assay:
≥75% (SDS-PAGE)
Recombinant:
expressed in Sf9 cells
General description
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.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
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
Long Zhang et al.
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
Yi-Chen Chen et al.
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
Atsushi Nagai et al.
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
Ping-Chung Chen et al.
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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