Abcam, ab198421, Recombinant human USP5 protein

Size: 50µg
Recombinant human USP5 protein is a Human Full Length protein, in the 2 to 858 aa range, expressed in Baculovirus infected Sf9 cells, with >55%, suitable for SDS-PAGE, FuncS.
Key facts
Purity:>55% SDS-PAGE,
Expression system:Baculovirus infected Sf9 cells,
Tags: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: 786 pmol/min/μgAssay Conditions: Reaction was performed in 50 mM Tris, pH 7.4, 1 mM DTT, 0.5 mM EDTA, 500 nM Ub-AMC, and ab198421 in a 50 μL reaction. Reaction was incubated at 37°C for 15 min. and fluorescent signal was measured at excitation = 340 nm, emission = 460 nm.,
Accession:P45974,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.71% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 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.
The target USP5 also known as ubiquitin-specific protease 5 or isopeptidase T functions as a deubiquitinating enzyme. This protein has a mass of about 169 kDa and plays a critical role in removing ubiquitin moieties from ubiquitin-conjugated protein substrates. USP5 achieves this by cleaving at the ubiquitin C-terminal glycine which releases free ubiquitin and recycles it for future use. Expression of USP5 occurs broadly throughout different tissues indicating its general importance in cellular processes.
Biological function summary
This enzyme helps maintain ubiquitin homeostasis by disassembling unanchored polyubiquitin chains. USP5 is not known to be part of a larger complex but it interacts with components of the ubiquitin-proteasome system contributing to protein quality control. By processing unanchored ubiquitin chains USP5 ensures a sufficient supply of ubiquitin preventing potential cellular stress due to ubiquitin depletion.
Pathways
USP5 integrates into the ubiquitin-proteasome pathway and proteostasis network. It collaborates with other deubiquitinating enzymes like USP14 and UCHL5 modulating the degradation of polyubiquitinated proteins. These pathways play essential roles in regulating protein turnover and disruptions in these processes can impact cell cycle and apoptosis highlighting the importance of USP5 in maintaining cellular homeostasis.
Experimental findings suggest USP5 involvement in several cancers and neurodegenerative diseases such as Alzheimer's disease. In cancer altered USP5 activity can disrupt the balance between protein synthesis and degradation promoting tumor progression. In Alzheimer's its role in ubiquitin homeostasis implicates it in the management of protein aggregates that characterize the disorder. USP5's relationship with other proteins like p53 in cancer and tau in Alzheimer's provides critical insights into its potential as a therapeutic target.