UCHL3 protein-HIS Epitope
Description
Background
UCHL3 or ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase) is a member of the deubiquitinating enzyme family that catalyze the removal of ubiquitin from polypeptides. The deubiquitinating enzyme family is divided into five classes, depending on the mechanism of catalysis. UCHL3 has been implicated in the etiology of neurodegeneration (1). UCHL3 may hydrolyze the ubiquitinyl-N-epsilon amide bond of ubiquitinated proteins to regenerate ubiquitin for another catalytic cycle and UCHL3 genes contain a conserved CpG island (2). UCHL1 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cell Cycle, Cellular Stress, Inflammation, Invasion/Metastasis, and Neurobiology research.
Application Note
UCHL3 Protein is stored in 50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol. UCHL3 Protein is suitable for use in Western Blot. Expect a band approximately ~27kDa on specific lysates or tissues. Specific conditions for reactivity should be optimized by the end user.
Purity/Specificity
Recombinant full-length human UCHL3 was expressed by E. coli cells using an N-terminal his epitope. The purity was determined to be >95% by densitometry.
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