Produced from human cDNA, expressed in E. coli. Ubiquitin C-terminal hydrolases (UCHs) are a family of cysteine hydrolases that catalyze the hydrolysis of amides, esters and thioesters of the C-terminus of ubiquitin. Mammalian neuronal cells abundantly express a deubiquitylating enzyme, ubiquitin carboxy-terminal hydrolase 1 (UCH-L1). Mutations in UCH-L1 are linked to Parkinson′s disease as well as gracile axonal dystrophy (gad) in mice. In contrast to the universally expressed UCH-L3 isozyme, UCH-L1 is expressed exclusively in neurons and testis/ovary. It has been shown that UCH-L1 associates and co-localizes with monoubiquitin and elongates ubiquitin half-life and the suggestion is made that UCH-L1, with avidity and affinity for ubiquitin, ensures ubiquitin stability within neurons.

Product Source: Recombinant human UCH-L1 expressed in E. coli

As supplied, store at -80°C for up to 12 months from date of receipt. Avoid repeated freeze/thaw cycles. After initial defrost, aliquot (for extended storage it is recommended that aliquots be no smaller then 10 μL) and store at -80°C. Snap-freezing in a dry ice/ethanol bath or liquid nitrogen is recommended. As supplied, the enzyme is stable on ice for several hours.

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