Recombinant Human His6-USP7 Protein, CF
Recombinant Human His6-USP7 Protein, CF Summary
Contains an N-terminal 6-His tag
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.
X mg/ml (X µM) in 50 mM HEPES pH 7.5, 100 mM NaCl, 1 mM TCEP
|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.
Ubiquitin Specific Peptidase 7 (USP7), also known as Herpes Virus-associated Ubiquitin Specific Protease (HAUSP), is a widely expressed deubiquitinating enzyme belonging to the peptidase C19 family (1). It has a predicted molecular weight of 130 kDa (2). Human USP7 is 1102 amino acids (aa) in length and shares 99% aa sequence identity with the mouse and rat orthologs (2,3). USP7 consists of a cysteine peptidase core (aa 208-560) that is flanked by an N-terminal TRAF-like domain (aa 50-205) and two C-terminal protease-resistant domains (aa 622-801 and 885-1061) (2,3). USP7 can be phosphorylated at Ser18 and Ser963 and ubiquitinated at Lys869 (2,4). USP7 was initially identified as a p53-interacting protein that deubiquitinates p53, thereby stabilizing the protein and inducing p53-dependent cell growth arrest and apoptosis (5). USP7 also targets the p53 regulatory proteins MDM2, MDMX, and Daxx, the epigenetic regulator Histone 2B, and the transcription factor FoxO4 (4,6-10). Additionally, USP7 interacts with the HSV-1 immediate early protein ICP0, contributing to the stabilization and transactivation capability of ICP0 during HSV-1 infection (1,11,12).
- Everett, R.D. et al. (1997) EMBO J. 16:1519.
- Fernández-Montalván, A. et al. (2007) FEBS J. 274:4256.
- Holowaty, M.N. et al. (2003) J. Biol. Chem. 278:47753.
- Khoronenkova, S.V. et al. (2012) Mol. Cell 45:801.
- Li, M. et al. (2002) Nature 416:648.
- Brooks, C.L. & W. Gu (2004) Cell Cycle 3:895.
- Meulmeester, E. et al. (2005) Cell Cycle 4:1166.
- Tanga, J. et al. (2010) Biochem. Biophys. Res. Commun. 393:542.
- van der Knaap, J.A. et al. (2005) Mol. Cell 17:695.
- van der Horst, A. et al. (2006) Nat. Cell Biol. 8:1043.
- Everett, R.D. et al. (1999) J. Virol. 73:417.
- Boutell, C. et al. (2005) J. Virol. 79:12342.
Citations for Recombinant Human His6-USP7 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.
Citations: Showing 1 - 4
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Regulation of transcriptional activators by DNA-binding domain ubiquitination
Authors: V Landré, B Revi, MG Mir, C Verma, TR Hupp, N Gilbert, KL Ball
Cell Death Differ., 2017;0(0):.
Sample Types: Cell Lysates
Discovery and characterization of highly potent and selective allosteric USP7 inhibitors
Authors: G Gavory, CR O'Dowd, MD Helm, J Flasz, E Arkoudis, A Dossang, C Hughes, E Cassidy, K McClelland, E Odrzywol, N Page, O Barker, H Miel, T Harrison
Nat. Chem. Biol., 2017;0(0):.
Sample Types: Cell Lysates
DNA damage shifts circadian clock time via Hausp-dependent Cry1 stabilization.
Authors: Papp, Stephani, Huber, Anne-Lau, Jordan, Sabine D, Kriebs, Anna, Nguyen, Madelena, Moresco, James J, Yates, John R, Lamia, Katja A
Sample Types: Whole Cells
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;10(4):298-304.
Sample Types: Protein
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