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| Product Name | Ubiquitin Specific Peptidase 5 (USP5) protein |
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| Description | 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. |
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| Size | 25 µg |
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| Concentration | n/a |
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| Applications | SDS-PAGE (SDS) |
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| Other Names | ISOT|AA407472|ISOT-1|Ucht |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | ABIN2745730 |
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| Order / More Info | Ubiquitin Specific Peptidase 5 (USP5) protein from ANTIBODIES-ONLINE GmbH |
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| Product Specific References | n/a |
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