USP7 / HAUSP Protein (GST Tag)

USP7 / HAUSP Protein Datasheet

USP7 / HAUSP Protein Product Information

• Synonym: HAUSP, TEF1
• Protein Construction: A DNA sequence encoding full length of human USP7 ( NP_003461.2 ) ( Met 1- Asn 1102 ) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus
• Source: Human
• Expression Host: Baculovirus-Insect cells

USP7 / HAUSP Protein QC Testing

• Purity: > 90 % as determined by SDS-PAGE
• Bio-activity: Measured by its binding ability in a functional ELISA
  Immobilized human P53 at 2 μg/ml ( 100 μl/well ) can bind human USP7 with a linear ranger of 6.4 - 160 ng/ml
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: The recombinant human USP7/GST chimera consists of 1339 amino acids and has a calculated molecular mass of 156 kDa. It migrates as an approximately 140 band in SDS-PAGE under reducing conditions
• Formulation: Lyophilized from sterile 50mM Tris 100mM NaCl, pH 8.0
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: USP7 protein

USP7 / HAUSP Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

USP7 / HAUSP Protein Description

Ubiquitin carboxyl-terminal hydrolase 7, also known as Ubiquitin thioesterase 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin-specific-processing protease 7, USP7 and HAUSP, is a widely expressed protein which belongs to the peptidase C19 family. USP7 is a member of the family of deubiquitinating enzymes. It is involved in the regulation of stress response pathways, epigenetic silencing and the progress of infections by DNA viruses. USP7 is a protein with a cysteine peptidase core, N- and C-terminal domains required for protein-protein interactions. USP7 contributes to epigenetic silencing of homeotic genes by Polycomb (Pc). USP7 cleaves ubiquitin fusion protein substrates. It deubiquitinates TP53/p53 and MDM2 and strongly stabilizes TP53 even in the presence of excess MDM2. USP7 also induces TP53-dependent cell growth repression and apoptosis. USP7 has key roles in the p53 pathway whereby it stabilizes both p53 and MDM2. Herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 stimulates lytic infection and the reactivation of quiescent viral genomes. ICP0 interacts very strongly with USP7. USP7-mediated stabilization of ICP0 is dominant over ICP0-induced degradation of USP7 during productive HSV-1 infection. The biological significance of the ICP0-USP7 interaction may be most pronounced in natural infection situations, in which limited amounts of ICP0 are expressed.

References

1. van der Knaap, et al., 2005, J.A. Mol Cell. 17 (5): 695-707.
2. Boutell, C. et al., 2005, J Virol. 79 (19): 12342-54.
3. Sheng, Y. et al., 2006, Nat Struct Mol Biol. 13 (3): 285-91.
4. Fernández-M, A. et al., 2007, FEBS J. 274 (16): 4256-70.
5. Antrobus, R. et al., 2008, Virus Res. 137 (1): 64-71.