Recombinant Human USP14/TGT Protein

Beta LifeScience SKU/CAT #: BLA-9536P

Recombinant Human USP14/TGT Protein

Beta LifeScience SKU/CAT #: BLA-9536P
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Product Overview

Host Species Human
Accession P54578
Synonym Deubiquitinating enzyme 14 TGT tRNA guanine transglycosylase tRNA guanine transglycosylase 60 kD subunit Ubiquitin carboxyl terminal hydrolase 14 Ubiquitin carboxyl-terminal hydrolase 14 Ubiquitin specific peptidase 14 Ubiquitin specific processing protease 14 Ubiquitin specific protease 14 Ubiquitin thiolesterase 14 Ubiquitin-specific-processing protease 14 UBP14_HUMAN USP 14 USP14
Description Recombinant Human USP14/TGT Protein was expressed in E.coli. It is a Full length protein
Source E.coli
AA Sequence MGSSHHHHHH SSGLVPRGSH MGSMPLYSVT VKWGKEKFEG VELNTDEPPM VFKAQLFALT GVQPARQKVM VKGGTLKDDD WGNIKIKNGM TLLMMGSADA LPEEPSAKTV FVEDMTEEQL ASAMELPCGL TNLGNTCYMN ATVQCIRSVP ELKDALKRYA GALRASGEMA SAQYITAALR DLFDSMDKTS SSIPPIILLQ FLHMAFPQFA EKGEQGQYLQ QDANECWIQM MRVLQQKLEA IEDDSVKETD SSSASAATPS KKKSLIDQFF GVEFETTMKC TESEEEEVTK GKENQLQLSC FINQEVKYLF TGLKLRLQEE ITKQSPTLQR NALYIKSSKI SRLPAYLTIQ MVRFFYKEKE SVNAKVLKDV KFPLMLDMYE LCTPELQEKM VSFRSKFKDL EDKKVNQQPN TSDKKSSPQK EVKYEPFSFA DDIGSNNCGY YDLQAVLTHQ GRSSSSGHYV SWVKRKQDEW IKFDDDKVSI VTPEDILRLS GGGDWHIAYV LLYGPRRVEI MEEESEQ
Molecular Weight 59 kDa including tags
Purity Greater than 90% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. 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. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation.
Subcellular Location Cytoplasm. Cell membrane; Peripheral membrane protein.
Protein Families Peptidase C19 family, USP14/UBP6 subfamily
Database References

Gene Functions References

  1. By displacing USP14, TRIM11 changes proteasome composition and suppresses both catalytic and non-catalytic effects of USP14 PMID: 29581427
  2. Usp14 and Ube3c cycle together on and off proteasomes, and the presence of ubiquitinated substrates promotes their association. This mechanism enables proteasome activity to adapt to the supply of substrates. PMID: 28396413
  3. Study detected elevated USP14 expression at both mRNA and protein levels, and was significantly associated with distant metastasis. PMID: 28509417
  4. These findings suggested that USP14 induces NF-kappaB activity and ERK1/2 phosphorylation triggered by microbial infection. PMID: 28364380
  5. Ubiquitin-specific protease 14 regulates cell proliferation and apoptosis in oral squamous cell carcinoma PMID: 27592452
  6. our report demonstrates significant value in targeting USP14/UCHL5 with VLX1570 in drug-resistant Waldenstrom macroglobulinemia (WM) and carries a high potential for clinical translation PMID: 27813535
  7. USP14 promotes prostate cancer progression. PMID: 28151478
  8. without a ubiquitinated substrate present, Usp14 suppresses multiple proteasomal activities, especially basal ATP consumption and degradation of non-ubiquitinated proteins. These allosteric effects thus reduce ATP hydrolysis by inactive proteasomes and nonspecific proteolysis and enhance proteasomal specificity for ubiquitinated proteins. PMID: 28416611
  9. USP14 regulates autophagy by negatively controlling K63 ubiquitination of Beclin 1 PMID: 27542828
  10. USP14 plays an important role in the progression and metastasis of esophageal squamous cell carcinoma. PMID: 27629392
  11. USP14 participates in CAM-DR of MM through acting as a bridge between Bcl-xl apoptotic pathway and Wnt-signaling pathways and may be represented as a good candidate for pursuing clinical trials in MM. PMID: 26710889
  12. Results show that USP14 mRNA is overexpressed in hepatocellular carcinoma (HCC) tissues and inversely correlates with miR-4782-3p level which binds to USP14 3'UTR to regulate its expression. PMID: 26782643
  13. Results found USP14 amplification and overexpression in many different cancers. Its overexpression in low-expression cell lines promoted cell proliferation and migration, whereas its downregulation suppressed tumor cell proliferation, increased apoptosis rate, and decreased cell migration and invasion suggesting an oncogenic role in various types of cancer. PMID: 26938858
  14. Increased USP14 expression in patients with breast cancer was associated with a poorer prognosis. PMID: 26712154
  15. Akt-mediated phosphorylation of USP14 at Ser432, which normally blocks its catalytic site in the inactive conformation, activates its deubiquitinating activity in vitro and in cells. PMID: 26523394
  16. our findings suggested that USP14 is involved in the progression of hepatocellular carcinoma(HCC) and may be a useful therapeutic target in HCC PMID: 26397990
  17. Cell surface ubiquitination precedes endocytosis, after which USP14 acts as an ubiquitin-binding protein that targets the ubiquitinated GABA B receptor to lysosomal degradation and promotes its deubiquitination. PMID: 26817839
  18. USP14 shows a marked preference for ubiquitin-cyclin B conjugates that carry more than one ubiquitin modification or chain PMID: 27074503
  19. our findings suggest that USP14 is involved in the progression of epithelial ovarian cancer PMID: 25429837
  20. Downregulation of USP14 expression arrested the cell cycle, which may be related to beta-catenin degradation. PMID: 23702845
  21. b-AP15 is an inhibitor of deubiquitylating enzyme USP14 and UCHL5 induces apoptosis in multiple myeloma and overcomes bortezomib resistance. PMID: 24319254
  22. overexpression of HA-USP14 increased the LPS-, TNFalpha-, or Escherichia coli-induced IL-8 release in human lung epithelial cells. PMID: 23615914
  23. the decrease in proteolysis of proteasomal substrates during aging is independent of the increased USP14 activity and that the reciprocal regulation of USP14 and proteasomal catalytic activity may be necessary to maintain cellular ubiquitin homeostasis. PMID: 23291607
  24. High Ubiquitin-specific protease 14 expression associated with intrahepatic cholangiocarcinoma cell differentiation. PMID: 21627382
  25. the catalytic cleft leading to the active site of USP14 is blocked by two surface loops. Binding by ubiquitin induces a significant conformational change thereby allowing access of the ubiquitin C-terminus to the active site. PMID: 16211010
  26. Results show the overall survival rate was worse in patients with a high USP14/TGT60 kD expression level and suggest that USP14/TGT60 kD also controls the fate of proteins that regulate tumor invasion and metastasis. PMID: 16465409
  27. Neuronal expression of full-length USP14 is able to restore the levels of monomeric ubiquitin in the brains of transgenic ataxia mice. PMID: 17079671
  28. USP14 were over-expressed in ovarian serous cystadenocarcinoma tissues, suggesting that the activity of ubiquitin-proteasome system is obviously enhanced in ovarian cancer. PMID: 17553343
  29. These findings suggest that USP14 is a novel player in the unfolded protein response by serving as a physiological inhibitor of ER-associated degradation under the non-stressed condition. PMID: 19135427
  30. Data from transgenic mice define a critical role for Usp14 at mammalian synapses and suggest a requirement for local ubiquitin recycling by the proteasome to control the development and function of neuromuscular junctions. PMID: 19726649

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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