|Other Names||Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, 6---, Neuron cytoplasmic protein 95, PGP 95, PGP95, Ubiquitin thioesterase L1, UCHL1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2126a was selected from the Park5 region of human UCHL1 (Park5) . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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||Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity.|
|Cellular Location||Cytoplasm. Endoplasmic reticulum membrane; Lipid-anchor. Note=About 30% of total UCHL1 is associated with membranes in brain|
|Tissue Location||Found in neuronal cell bodies and processes throughout the neocortex (at protein level). Expressed in neurons and cells of the diffuse neuroendocrine system and their tumors Weakly expressed in ovary. Down-regulated in brains from Parkinson disease and Alzheimer disease patients|
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Provided below are standard protocols that you may find useful for product applications.
Ubiquitin is a 76 amino acid highly conserved eukaryotic polypeptide that selectively marks cellular proteins for proteolytic degradation by the 26S proteasome. The process of target selection, covalent attachment and shuttle to the 26S proteasome is a vital means of regulating the concentrations of key regulatory proteins in the cell by limiting their lifespans. Polyubiquitination is a common feature of this modification. Serial steps for modification include the activation of ubiquitin, an ATP-dependent formation of a thioester bond between ubiquitin and the enzyme E1, transfer by transacylation of ubiquitin from E1 to the ubiquitin conjugating enzyme E2, and covalent linkage to the target protein directly by E2 or via E3 ligase enzyme. Deubiquitination enzymes also exist to reverse the marking of protein substrates. Posttranslational tagging by Ub is involved in a multitude of cellular processes, including the cell cycle, cell growth and differentiation, embryogenesis, apoptosis, signal transduction, DNA repair, regulation of transcription and DNA replication, transmembrane transport, stress responses, the immune response, and nervous system functions.
Maraganore, D.M., et al., Mov Disord 18(6):631-636 (2003).Nishikawa, K., et al., Biochem. Biophys. Res. Commun. 304(1):176-183 (2003).Liu, Y., et al., Cell 111(2):209-218 (2002).Caballero, O.L., et al., Oncogene 21(19):3003-3010 (2002).Saigoh, K., et al., Nat. Genet. 23(1):47-51 (1999).
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