Rabbit Isopeptidase T/USP5 Protein, CF
Rabbit Isopeptidase T/USP5 Protein, CF Summary
Product Specifications
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
E-320
| Formulation | X mg/ml (X μM) in 50 mM HEPES pH 8.0, 150 mM NaCl, 1mM DTT |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Isopeptidase T/USP5
Isopeptidase T/Ubiquitin Specific Peptidase 5 (USP5) is a widely expressed deubiquitinating enzyme belonging to the peptidase C19 family (1). It is the only known member that requires zinc binding to be active (2). It has a predicted molecular weight of 95.8 kDa (3). Human Isopeptidase T/USP5 is 858 amino acids (aa) in length and shares 98% aa sequence identity with the mouse and rat orthologs (3). 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 (1,4,5). 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) (5-7). 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 (5,6,8). 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 (5,7). There are short and long forms of human Isopeptidase T/USP5 that differ by an insertion of 23 aa in the long form (2). 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 (9). Conversely, an up-regulation of USP5 has been associated with fetal Down syndrome (10).
- Wilkinson, K.D. et al. (1995) Biochemistry 34:14535.
- Gabriel, J.M. et al. (2002) Biochemistry 41:13755.
- Falquet, L. et al. (1995) FEBS Lett. 376:233.
- Raasi, S. et al. (2005) Nat. Struct. Mol. Biol. 12:708.
- Reyes-Turcu, F.E. et al. (2009) Annu. Rev. Biochem. 78:363.
- Reyes-Turcu, F.E. et al. (2006) Cell 124:1197.
- Reyes-Turcu, F.E. et al. (2008) J. Biol. Chem. 283:19581.
- Avvakumov, G.V. et al. (2012) Biochemistry 51:1188.
- Dayal, S. et al. (2009) J. Biol. Chem. 284:5030.
- Engidawork, E. et al. (2001) J. Neural Transm. Suppl.(61):117.
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