Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, 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 Parkinsons, Alzheimers, and Huntingtons disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
Lyophilized from a 0.22 µm filtered solution of 20mM Tris-HCl, 250mM NaCl, 0.05% Tween80, 1mM DTT, pH 8.5.
Application Notes:
Cross-Reactivity: Centrifµge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage,it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA,5% HSA,10% FBS or 5% Trehalose),and aliquot the reconstituted protein solution to minimize free-thaw cycles. ResearchArea: Other Recombinant Protein
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