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Recombinant Human Isopeptidase T/USP5 Protein, CF

Catalog #: E-322
3 Citations Datasheet / COA / SDS

Discontinued Product

E-322 has been discontinued.
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Recombinant Human Isopeptidase T/USP5 Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Activity
Recombinant Human Isopeptidase T/USP5 is a Ubiquitin-specific deconjugating enzyme. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human Isopeptidase T/USP5 concentration of 10-100 nM.  A 15 minute pre-incubation with 10 mM DTT is recommended to achieve maximum activity.
Source
E. coli-derived human Isopeptidase T/USP5 protein
Accession #
P45974
Predicted Molecular Mass
96 kDa

Product Datasheets

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E-322

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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-322

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.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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).

References
  1. Wilkinson, K.D. et al. (1995) Biochemistry 34:14535.
  2. Gabriel, J.M. et al. (2002) Biochemistry 41:13755.
  3. Falquet, L. et al. (1995) FEBS Lett. 376:233.
  4. Raasi, S. et al. (2005) Nat. Struct. Mol. Biol. 12:708.
  5. Reyes-Turcu, F.E. et al. (2009) Annu. Rev. Biochem. 78:363.
  6. Reyes-Turcu, F.E. et al. (2006) Cell 124:1197.
  7. Reyes-Turcu, F.E. et al. (2008) J. Biol. Chem. 283:19581.
  8. Avvakumov, G.V. et al. (2012) Biochemistry 51:1188.
  9. Dayal, S. et al. (2009) J. Biol. Chem. 284:5030.
  10. Engidawork, E. et al. (2001) J. Neural Transm. Suppl.(61):117.
Long Name
Ubiquitin Specific Protease 5
Entrez Gene IDs
8078 (Human); 22225 (Mouse); 297593 (Rat)
Alternate Names
Deubiquitinating enzyme 5; EC 3.1.2.15; EC 3.4.19.12; Isopeptidase T; IsoT; ISOTubiquitin carboxyl-terminal hydrolase 5; ubiquitin isopeptidase T; ubiquitin specific peptidase 5 (isopeptidase T); ubiquitin specific protease 5 (isopeptidase T); ubiquitin thioesterase 5; Ubiquitin thiolesterase 5; ubiquitin-specific protease-5 (ubiquitin isopeptidase T); Ubiquitin-specific-processing protease 5; USP5

Citations for Recombinant Human Isopeptidase T/USP5 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. OTULIN limits cell death and inflammation by deubiquitinating LUBAC
    Authors: K Heger, KE Wickliffe, A Ndoja, J Zhang, A Murthy, DL Dugger, A Maltzman, F de Sousa E, J Hung, Y Zeng, E Verschuere, DS Kirkpatric, D Vucic, WP Lee, M Roose-Girm, RJ Newman, S Warming, YC Hsiao, LG K?m?ves, JD Webster, K Newton, VM Dixit
    Nature, 2018-06-27;559(7712):120-124.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Bioassay
  2. Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions
    Nat Commun, 2016-11-16;7(0):13288.
    Applications: Bioassay
  3. A selective USP1-UAF1 inhibitor links deubiquitination to DNA damage responses.
    Authors: Liang, Qin, Dexheimer, Thomas S, Zhang, Ping, Rosenthal, Andrew S, Villamil, Mark A, You, Changjun, Zhang, Qiuting, Chen, Junjun, Ott, Christin, Sun, Hongmao, Luci, Diane K, Yuan, Bifeng, Simeonov, Anton, Jadhav, Ajit, Xiao, Hui, Wang, Yinsheng, Maloney, David J, Zhuang, Zhihao
    Nat Chem Biol, 2014-02-16;10(4):298-304.
    Applications: Bioassay

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