Recombinant Human USP14/TGT protein (Tagged) is a Human Full Length protein, in the 1 to 494 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029).
TGT, USP14, Ubiquitin carboxyl-terminal hydrolase 14, Deubiquitinating enzyme 14, Ubiquitin thioesterase 14, Ubiquitin-specific-processing protease 14
Recombinant Human USP14/TGT protein (Tagged) is a Human Full Length protein, in the 1 to 494 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029).
Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
USP14 also known as Ubiquitin Specific Peptidase 14 is a deubiquitinating enzyme that plays a mechanical role in the ubiquitin-proteasome system. This enzyme has a molecular mass around 56 kDa and is essential for proteasome-mediated degradation activities. It is broadly expressed across many tissues but shows significant presence in the nervous system. Often people refer to USP14 as TGT in the context of certain studies or databases.
USP14 functions in regulating protein turnover by removing ubiquitin from substrate proteins impacting their stability and degradation. USP14 is part of a larger protein complex associated with the proteasome specifically binding to the 19S regulatory particle. It is important in maintaining cellular protein homeostasis by editing ubiquitin chains on target proteins prior to degradation.
USP14 participates in ubiquitin-proteasome pathways and ER-associated degradation pathway. In these processes it works closely with other proteasome proteins such as Rpn11 which also removes ubiquitin from proteins. The regulation of these pathways by USP14 directly affects protein quality control in cells influencing processes like cell cycle and stress response.
USP14 has associations with neurodegenerative diseases such as Alzheimer's and Parkinson’s. It affects disease progression by modulating levels of proteins that aggregate in these conditions. Connections between USP14 and proteins such as tau and α-synuclein highlight its contribution to the pathological features seen in these disorders. Further research into USP14's role may help to uncover new therapeutic strategies for these diseases.
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SDS-PAGE analysis of ab269115.
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