|Application ||WB, IHC-P, E|
|Reactivity||Human, Mouse, Rat|
|Dilution||ELISA (1:5000), IHC-P (5 µg/ml), WB (1:500-1:1000)|
|Other Names||Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, 220.127.116.11, 6.-.-.-, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1, UCHL1|
|Target/Specificity||PGP9.5 Antibody detects endogenous levels of total PGP9.5 protein.|
|Reconstitution & Storage||Store at -20°C.|
|Precautions||UCHL1 / PGP9.5 Antibody (aa171-220) 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|
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Provided below are standard protocols that you may find useful for product applications.
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.
Hillier L.W.,et al.Nature 434:724-731(2005).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Day I.N.M.,et al.Biochem. J. 268:521-524(1990).
Choi J.,et al.J. Biol. Chem. 279:13256-13264(2004).
Lubec G.,et al.Submitted (DEC-2008) to UniProtKB.
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