Name :
Recombinant Human UCHL1 Protein (His Tag)
Biological Activity :
Background :
Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is 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. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson’s, Alzheimer’s, and Huntington’s disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
Biological Activity :
Measured by the hydrolysis of UbiquitinAMC. The specific activity is >100 pmoles/min/μg.
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_004172.2
NCBI Gene ID :
Synonyms :
Synonyms :
ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)
Amino Acid Sequence :
Molecular Weight :
The recombinant human UCHL1 consisting of 229 amino acids and migrates as an 25.6 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity :
> 92 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the native human UCHL1 (NP_004172.2) (Gln 2-Ala 223) was expressed, with a polyhistide tag at the N-terminus.
Buffer Solution :
Supplied as sterile 20mM Tris, 500mM NaCl, 20% glycerol, 1mM DTT, pH 8.0Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
HEL-117 Protein, Human; NDGOA Protein, Human; PARK5 Protein, Human; PGP9.5 Protein, Human; PGP95 Protein, Human; UCH-L1 Protein, Human UCHL1 背景信息 Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is 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. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson’s, Alzheimer’s, and Huntington’s disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
References & Citations :
Wada H., et al., 1998, Biochem. Biophys. Res. Commun. 251:688-92. Choi J., et al., 2004, J. Biol. Chem. 279:13256-64. Lombardino,A.2005, et al., J.Proc Natl Acad Sci.USA102 (22):8036-41 Okochi-Takada,E. et al., 2006, Int J Cancer. 119 (6):1338-44. Zetterberg, M. et al., 2010, Mol Neurodegener 5 :11.
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