Recombinant human USP5 protein (Active) is a Human Full Length protein, expressed in Escherichia coli, with >70% purity and suitable for SDS-PAGE, FuncS.
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Key facts
- Purity
- >70% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.
Alternative names
ISOT, USP5, Ubiquitin carboxyl-terminal hydrolase 5, Deubiquitinating enzyme 5, Isopeptidase T, Ubiquitin thioesterase 5, Ubiquitin-specific-processing protease 5
Recommended products
Recombinant human USP5 protein (Active) is a Human Full Length protein, expressed in Escherichia coli, with >70% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >70% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- ab269124 specific activity was determined to be 90 nmol/min/mg in a DUB assay using recombinant human ubiquitin-based proluciferin substrate.
- Accession
- P45974-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 7
Preservative: 1.02% Imidazole
Constituents: 25% Glycerol (glycerin, glycerine), 1.74% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF
Sequence info
Amino acid sequence
- Accession
- P45974
- Protein length
- Full Length
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
General info
- Function
Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.
- Sequence similarities
Belongs to the peptidase C19 family.
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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.
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2 product images
Functional Studies - Recombinant human USP5 protein (Active) (ab269124)
ab269124 specific activity was determined to be 90 nmol/min/mg in a DUB assay using recombinant human ubiquitin-based proluciferin substrate.
SDS-PAGE - Recombinant human USP5 protein (Active) (ab269124)
SDS-PAGE analysis of ab268124.
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