Abcam, ab198464, Recombinant human HAUSP / USP7 protein

Size: 100µg
Recombinant human HAUSP / USP7 protein is a Human Full Length protein, in the 2 to 1102 aa range, expressed in Baculovirus infected Sf9 cells, with >66%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.
Key facts
Purity:>66% SDS-PAGE,
Endotoxin level:< 1 EU/µg,
Expression system:Baculovirus infected Sf9 cells,
Tags:His-DDDDK tag N-Terminus,
Applications:FuncS, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity: 545 pmol/min/μgAssay Conditions: Reaction was performed in 50 mM Tris pH 7.4, 1 mM DTT. 0.5 mM EDTA, and 500 nM Ub-AMC. Reaction was incubated at 37°C for 15 min. and fluorescent signal was measured at excitation of 340 nm, and emission at 460 nm.,
Accession:Q93009,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Preservative: 0.61% ImidazoleConstituents: 5% Glycerol (glycerin, glycerine), 0.76% Sodium chloride, 0.75% Tris HCl, 0.02% Potassium chloride

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
HAUSP also known as USP7 is a deubiquitinating enzyme with a molecular mass of approximately 135 kDa. It functions by removing ubiquitin molecules from target proteins influencing their stability and activity. HAUSP is widely expressed in various human tissues with notable presence in the nucleus and cytoplasm. Its expression is essential for modulation of multiple signaling pathways. The enzyme's capacity to regulate protein ubiquitination dynamics makes it a significant player in cellular function.
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.
HAUSP has implications in cancer and neurodegenerative diseases. Aberrant activity or expression of HAUSP has been linked to tumorigenesis particularly through its interaction with the proteins p53 and MDM2 affecting cell survival and proliferation. In neurodegenerative conditions altered HAUSP activity may impact protein homeostasis and degradation pathways contributing to disease progression. Its connection to these proteins and disease states highlights its potential as a therapeutic target in associated disorders.