Recombinant human HAUSP / USP7 protein (Active)
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Recombinant human HAUSP / USP7 protein (Active) is a Human Fragment protein, in the 25 to 580 aa range, expressed in Escherichia coli, with >75%, suitable for SDS-PAGE, FuncS.
View Alternative Names
HAUSP, USP7, Ubiquitin carboxyl-terminal hydrolase 7, Deubiquitinating enzyme 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin thioesterase 7, Ubiquitin-specific-processing protease 7
- FuncS
Supplier Data
Functional Studies - Recombinant human HAUSP / USP7 protein (Active) (AB269127)
ab269127 specific activity was determined to be 4 nmol/mon/mg in a DUB assay using recombinant human ubiquitin-based proluciferin substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human HAUSP / USP7 protein (Active) (AB269127)
SDS-PAGE analysis of ab269127.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
HAUSP influences several critical cellular processes including DNA repair transcriptional regulation and cell cycle progression. It often interacts with other proteins such as p53 to modify their functions by altering their ubiquitination status. HAUSP does not function in isolation but forms part of larger protein complexes where it plays a role in processing substrate proteins. Its ability to activate or deactivate proteins through deubiquitination highlights its importance in maintaining cellular homeostasis.
Pathways
Research identifies HAUSP as an important component in both the p53 pathway and the Wnt signaling pathway. Through the p53 pathway HAUSP directly interacts with the p53 tumor suppressor protein influencing cell cycle and apoptosis decisions. Its participation in the Wnt signaling pathway associates it with beta-catenin where it supports cellular proliferation and differentiation. These pathway interactions illustrate HAUSP's integral role in maintaining cellular function and responding to various signaling inputs.
Specifications
Form
Liquid
General info
Function
Hydrolase that deubiquitinates target proteins such as FOXO4, DEPTOR, KAT5, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed : 11923872, PubMed : 15053880, PubMed : 16964248, PubMed : 18716620, PubMed : 25283148, PubMed : 25865756, PubMed : 26678539, PubMed : 28655758, PubMed : 35216969). 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, PubMed : 26786098). 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). Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins (PubMed : 27123980). Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells (PubMed : 21258371). Deubiquitinates SIRT7, inhibiting SIRT7 histone deacetylase activity and regulating gluconeogenesis (PubMed : 28655758). Involved in the regulation of WASH-dependent actin polymerization at the surface of endosomes and the regulation of endosomal protein recycling (PubMed : 26365382). It maintains optimal WASH complex activity and precise F-actin levels via deubiquitination of TRIM27 and WASHC1 (PubMed : 26365382). Mediates the deubiquitination of phosphorylated DEPTOR, promoting its stability and leading to decreased mTORC1 signaling (PubMed : 35216969).. (Microbial infection) Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection.. (Microbial infection) Upon infection with Epstein-Barr virus, the interaction with viral EBNA1 increases the association of USP7 with PML proteins, which is required for the polyubiquitylation and degradation of PML.
Sequence similarities
Belongs to the peptidase C19 family.
Post-translational modifications
Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated.. 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.
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
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