|Other Accession||Q00981, Q6SEG5, Q9R0P9, Q60HC8, P23356|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||H=25;M=25;Rat=25 KDa|
|Other Names||UCHL1; Ubiquitin carboxyl-terminal hydrolase isozyme L1; Neuron cytoplasmic protein 9.5; PGP 9.5; Ubiquitin thioesterase L1|
|Target/Specificity||This UCHL1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 187-216 amino acids from the C-terminal region of human UCHL1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||UCHL1 Antibody (C-term) is for research use only and 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|
UCHL1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCHL1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. It is present in all neurons (Doran et al., 1983 [PubMed 6343558]).
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).