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|Product Name||USP14, 1-494aa Human|
|Amino Acid 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|
|Background||USP14 is a member of the ubiquitin-specific processing (UBP) family of proteases that is a deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the cytoplasm and cleaves the ubiquitin moiety from ubiquitin-fused precursors and ubiquitinylated proteins. Mice with a mutation that results in reduced expression of the ortholog of this protein are retarded for growth, develop severe tremors by 2 to 3 weeks of age followed by hindlimb paralysis and death by 6 to 10 weeks of age. Recombinant human USP14 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.|
|Concentration||1 mg/ml (determined by Bradford assay)|
|Form||Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.4M urea, 10% glycerol|
|Intended Use||For Research Use Only|
|Molecular Weight||20.2 kDa (186aa)|
|NCBI Accession #||NP_005142|
|Purity||> 90% by SDS-PAGE|
|References||Shinji S, Naito Z, et al. (2009). Oncol Rep. 15(3):539-43.
Mines MA, Goodwin JS, et al. (2009). J Biol Chem. 284(9):5742-52.
|Storage||Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.|
|Synonyms||Ubiquitin carboxyl-terminal hydrolase 14, TGT, Ubiquitin thioesterase 14|
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