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USP7/HAUSP  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: Baculovirus-Insect Cells  
11681-H20BL-50
11681-H20BL-100
50 µg 
100 µg 
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Expression host: Baculovirus-Insect Cells  
11681-H20B-50
11681-H20B-100
50 µg 
100 µg 
Add to Cart
  • Slide 1
Expression host: Baculovirus-Insect Cells  
11681-HNCB-50
11681-HNCB-100
50 µg 
100 µg 
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USP7/HAUSP Related Area

USP7/HAUSP Related Pathways

    USP7/HAUSP Related Protein, Antibody, cDNA Gene, and ELISA Kits

    USP7/HAUSP Summary & Protein Information

    USP7/HAUSP Background

    Gene Summary: OMIM - description for USP7 (HAUSP):
    General information above from NCBI
    Catalytic activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
    Enzyme regulation: ENZYME REGULATION: Inhibited by N-ethyl-maleimide (NEM) and divalent cations. Tolerates high concentrations of NaCl but is inhibited at concentrations of 195 mM and higher. {ECO:0000269|PubMed:14506283}.
    Subunit structure: Monomer. Homodimer. Part of a complex with DAXX, MDM2, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts with MDM2; the interaction is independent of p53/TP53. Interacts with DAXX; the interaction is direct and independent of MDM2 and p53/TP53. Interacts with FOXO4; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of p53/TP53. Interacts with p53/TP53; the interaction is enhanced in response to DNA damage; the interaction is impaired by TSPYL5. Interacts with PTEN; the interaction is direct. Interacts with UBXN6. Interacts with ATXN1 and the strength of interaction is influenced by the length of the poly-Gln region in ATXN1. A weaker interaction seen with mutants having longer poly-Gln regions. Interacts with KIAA1530/UVSSA. Isoform 1 and isoform 2 interact with herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110. Interacts with Epstein-Barr virus EBNA1. EBNA1 shows a 10-fold higher affinity than p53/TP53 and can compete with it for USP7 binding. Binding to ICP0/VMW110 may modulate the substrate specificity or activity of USP7 to stabilize viral proteins. Interacts with MEX3C and antagonizes its ability to degrade mRNA. Interacts with DNMT1 and UHRF1. Interacts with FOXP3. Interacts (via MATH domain) with RNF220 (PubMed:25266658). {ECO:0000269|PubMed:11923872, ECO:0000269|PubMed:12093161, ECO:0000269|PubMed:12507430, ECO:0000269|PubMed:14506283, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15808506, ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:16402859, ECO:0000269|PubMed:16474402, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:16964248, ECO:0000269|PubMed:17651432, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:18590780, ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:18768758, ECO:0000269|PubMed:21170034, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:22411829, ECO:0000269|PubMed:22466611, ECO:0000269|PubMed:22466612, ECO:0000269|PubMed:22863774, ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:25266658}.
    Domain: The C-terminus plays a role in its oligomerization. {ECO:0000250}.
    Subcellular location: Nucleus {ECO:0000269|PubMed:23973222}. Cytoplasm. Nucleus, PML body. Note=Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies.
    Tissue specificity: Widely expressed. Overexpressed in prostate cancer. {ECO:0000269|PubMed:18716620}.
    Induction: Up-regulated in regulatory T-cells (Treg). {ECO:0000269|PubMed:23973222}.
    Post-translational: Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated. {ECO:0000269|PubMed:17651432}.; Isoform 1: Polyneddylated. Isoform 2: Not Polyneddylated.; Isoform 1 and isoform 2: Not sumoylated.; Isoform 1 and isoform 2: Polyubiquitinated by herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110; leading to its subsequent proteasomal degradation. Isoform 1: Ubiquitinated at Lys-869. {ECO:0000269|PubMed:16160161, ECO:0000269|PubMed:17651432}.
    Sequence similarity: Belongs to the peptidase C19 family. {ECO:0000305}.; Contains 1 MATH domain. {ECO:0000255|PROSITE-ProRule:PRU00129}.; Contains 1 USP domain. {ECO:0000305}.
    General information above from UniProt

    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.

    USP7/HAUSP Alternative Name

    USP7/HAUSP Related Studies

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