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Ubiquitin Specific Protease 5; USP5; IsoT; Ubiquitin Carboxyl-terminal Hydrolase 5; Deubiquitinating Enzyme 5; Ubiquitin Thioesterase 5

Protein

Rabbit Erythrocytes

Rabbit isopeptidase T.

Rabbit

~97kDa

≥95% (SDS-PAGE)

Liquid. In 50mM HEPES pH 8.0, 150mM NaCl, 1mM DTT.

Use: Ubiquitin-specific deconjugating enzyme. Reaction conditions will need to be optimized for each specific application. We recommend an initial enzyme concentration of 10-100nM. Pre-incubation (15min) with 10mM DTT is recommended to achieve maximum activity.

Manufactured by Boston Biochem

DRY ICE

-20°C

-80°C

Aliquot to avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -80°C.

No

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Isopeptidase T/Ubiquitin Specific Peptidase 5 (USP5) is a widely expressed deubiquitinating enzyme belonging to the peptidase C19 family. It is the only known member that requires zinc binding to be active. It has a predicted molecular weight of 95.8 kDa. Human Isopeptidase T/USP5 is 858 amino acids (aa) in length and shares 98% aa sequence identity with the mouse and rat orthologs. Isopeptidase T/USP5 is largely responsible for the disassembly of unanchored poly-ubiquitin chains. It binds multiple ubiquitin molecules in a poly-ubiquitin chain and can cleave Lys29-, Lys48- and Lys63-linked chains. It contains four putative ubiquitin-binding domains: an N-terminal zinc finger ubiquitin-binding (ZnF-UBP) domain, a ubiquitin-specific processing protease (UBP) catalytic domain, and two ubiquitin-associated domains (UBA1 and UBA2). The ZnF-UBP domain (aa 163-291) selectively interacts with an unmodified C-terminus of poly-ubiquitin chains and induces a conformational change that prevents Isopeptidase T/USP5 from disassembling poly-ubiquitin until another deubiquitinating enzyme has released the chain from the ubiquitinated protein. The UBP domain binds the second ubiquitin in poly-ubiquitin, while the subsequent ubiquitins bind the UBA2 (aa 722-762) and UBA1 (aa 654-695) domains. There are short and long forms of human Isopeptidase T/USP5 that differ by an insertion of 23 aa in the long form. Suppression of Isopeptidase T/USP5 has been shown to increase the amount and transcriptional activity of p53 due to the accumulation of unanchored poly-ubiquitin. Conversely, an up-regulation of USP5 has been associated with fetal down syndrome.