|Reactivity||Human, Mouse, Chicken|
|Calculated MW||128302 Da|
|Application & Usage||Western blotting (1:500 – 1:2000). However, the optimal concentrations should be determined individually. The antibody recognizes USP7 of human origin. HeLa cell nuclear extract can be used as a positive control. Based on sequence homology, the antibody should also react with mouse and chick samples. |
|Other Names||USP7, ubiquitin specific processing protease 7; HAUSP, Herpes virus-associated ubiquitin-specific protease; Deubiquitinating enzyme 7; Ubiquitin thiolesterase 7; Ubiquitin carboxyl-terminal hydrolase 7; TEF1|
|Formulation||100 µl affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 0.5% BSA and 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||USP7 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. 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. 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. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/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. 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. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. 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. Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. 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. 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.|
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Provided below are standard protocols that you may find useful for product applications.
Ubiquitin (Ub) is a highly conserved protein found ubiquitously in eukaryotic organisms. The conjugation of ubiquitin to proteins is an important means to regulate protein activity for many cellular processes by tagging them for degradation. Removal of Ub can rescue proteins from degradation. This is accomplished by the ubiquitin-specific processing protease (UBP) family of enzymes. Ubiquitin specific processing protease 7 (USP7) is a member of this family that has been shown to interact and stabilize p53.
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