UCHL3, Active, Recombinant, Human, His-Tag (Ubiquitin Carboxyl-terminal Hydrolase Isozyme L3, UCH-L3, Ubiquitin Thioesterase L3)

UCH-L3 (Ubiquitin carboxyterminal hydrolase isozyme 3) is a 26-28kD member of the peptidase C12 family of enzymes. It shows wide expression, being noted in adipocytes, renal duct epithelium, neurons, and striated muscle. UCH-L3 cleaves both monomeric ubiquitin (Ub) from Ub-protein conjugates, and a GGLRQ peptide from the C-terminus of the Ub-like protein NEDD-8. Notably, UCH-L3 activity is muted in the presence of Ub interacting dimers. Human UCH-L3 is 230aa in length. It is phosphorylated on Ser75 and Ser130, and contains two ubiquitin-binding sequences between aa40-57 and 178-186. Four potential splice forms have been reported. Two show a four aa deletion between aa15-18, with one also containing a 14aa substitution for aa179-230. Two others contain an alternative start site at Met37, one of which is also accompanied by a seven aa substitution for aa143-230. Full-length human UCH-L3 shares 98% aa identity with mouse and rat UCH-L3.\n\nSource:\nRecombinant corresponding to aa2-231 from human UCHL3, fused to His-tag at N-terminal, expressed in E. coli.\n\nMolecular Weight:\n~27.1kD\n\nApplications: \nSuitable for for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

137392

Size

100ug

Form

Supplied as a liquid in 45mM Tris-HCl, pH 8.0, 124mM sodium chloride, 2.4mM potassium chloride, 225mM imidazole, 10% glycerol, 3mM DTT.

Purity

Highly Purified (~95%)

References

1. Wada, H., et al. (1998). Biochem. Biophys. Res. Commun. 251 (3): 688-92. 2. Nam, M.J., et al. (2004). Proteomics 3 (11): 2108-15. 3. Setsuie, R., et al. (2009). Neurochem Int. 54(5-6):314-21.