|Other Names||Ubiquitin carboxyl-terminal hydrolase 4, Deubiquitinating enzyme 4, Ubiquitin thioesterase 4, Ubiquitin-specific-processing protease 4, Ubiquitous nuclear protein homolog, USP4, UNP, UNPH|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER.|
|Cellular Location||Cytoplasm. Nucleus Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor The relative amounts found in the nucleus and cytoplasm vary according to the cell type.|
|Tissue Location||Overexpressed in small cell tumors and adenocarcinomas of the lung compared to wild-type lung (at protein level). Expressed in the hippocampal neurons|
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Provided below are standard protocols that you may find useful for product applications.
Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. Plays a role in the regulation of quality control in the ER.
Morgan, A.R., et al. Hum. Immunol. 71(6):602-609(2010)So, H.C., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 153B (1), 103-113 (2010) :Zhao, B., et al. J. Cell. Mol. Med. 13 (8B), 1886-1895 (2009) :Milojevic, T., et al. Mol. Pharmacol. 69(4):1083-1094(2006)Wada, K., et al. Biochem. Biophys. Res. Commun. 342(1):253-258(2006)
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