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USP7 Antibody (Center)

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - USP7 Antibody (Center) AP16712c
    USP7 Antibody (Center) (Cat. #AP16712c) western blot analysis in A2058 cell line lysates (35ug/lane).This demonstrates the USP7 antibody detected the USP7 protein (arrow).
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q93009
Other Accession Q4VSI4, NP_003461.2
Reactivity Human
Predicted Rat
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 128302 Da
Additional info
Gene ID 7874
Other Names Ubiquitin carboxyl-terminal hydrolase 7, Deubiquitinating enzyme 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin thioesterase 7, Ubiquitin-specific-processing protease 7, USP7, HAUSP
Target/Specificity This USP7 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 320-348 amino acids from the Central region of human USP7.
Dilution WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsUSP7 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name USP7 (HGNC:12630)
Synonyms HAUSP
Function Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:26678539). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis (PubMed:25283148). Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis (PubMed:11923872). Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity (PubMed:16964248). In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML (PubMed:18716620). Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation (PubMed:26678539). Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC- NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6 (PubMed:22466611, PubMed:22466612). Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1 (PubMed:21745816, PubMed:22411829). Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (PubMed:20601937). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:20601937). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains (PubMed:22689415). Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222).
Cellular Location Nucleus Cytoplasm. Nucleus, PML body. Chromosome. 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 Location Widely expressed. Overexpressed in prostate cancer.
Research Areas

BACKGROUND

Hydrolase that deubiquitinates target proteins such as FOXO4, TP53, MDM2, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and proteasomal degradation. Deubiquitinates TP53 and MDM2 and strongly stabilizes TP53 even in the presence of excess MDM2, and also induces TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection.

REFERENCES

Sarkari, F., et al. J. Mol. Biol. 402(5):825-837(2010)
de Bie, P., et al. Biochem. Biophys. Res. Commun. 400(3):389-395(2010)
Maertens, G.N., et al. EMBO J. 29(15):2553-2565(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Tang, J., et al. Biochem. Biophys. Res. Commun. 393(3):542-545(2010)

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