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AB198421

Recombinant human USP5 protein (DDDDK tag N-Terminus)

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Recombinant human USP5 protein (DDDDK tag N-Terminus) 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.

View Alternative Names

ISOT, USP5, Ubiquitin carboxyl-terminal hydrolase 5, Deubiquitinating enzyme 5, Isopeptidase T, Ubiquitin thioesterase 5, Ubiquitin-specific-processing protease 5

2 Images
Functional Studies - Recombinant human USP5 protein (DDDDK tag N-Terminus) (AB198421)
  • FuncS

Supplier Data

Functional Studies - Recombinant human USP5 protein (DDDDK tag N-Terminus) (AB198421)

Activity assay using ab198421.

SDS-PAGE - Recombinant human USP5 protein (DDDDK tag N-Terminus) (AB198421)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human USP5 protein (DDDDK tag N-Terminus) (AB198421)

10% SDS-PAGE analysis of ab198421 (2.5 μg).

Key facts

Purity

>55% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

DDDDK tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: 786 pmol/min/μg

Assay 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: 8 Constituents: 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

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"AELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESEGGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTRRPKEEDPATGTGDPPRKKPTRLAIGVEGGFDLSEEKFELDEDVKIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSADSASRKQEVQAWDGEVRQVSKHAFSLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGSILCGRRYFDGSGGNNHAVEHYRETGYPLAVKLGTITPDGADVYSYDEDDMVLDPSLAEHLSHFGIDMLKMQKTDKTMTELEIDMNQRIGEWELIQESGVPLKPLFGPGYTGIRNLGNSCYLNSVVQVLFSIPDFQRKYVDKLEKIFQNAPTDPTQDFSTQVAKLGHGLLSGEYSKPVPESGDGERVPEQKEVQDGIAPRMFKALIGKGHPEFSTNRQQDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLATEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAEEEKMALPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAKSVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEMPEELDISQLRGTGLQPGEEELPDIAPPLVTPDEPKGSLGFYGNEDEDSFCSPHFSSPTSPMLDESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPGSSGPGSTSAAADPPPEDCVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDLDAEAAMDISEGRSAADSISESVPVGPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIKKEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVAS","proteinLength":"Full Length","predictedMolecularWeight":"96 kDa","actualMolecularWeight":null,"aminoAcidEnd":858,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"P45974","tags":[{"tag":"DDDDK","terminus":"N-Terminus"}]}]

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
True

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.

Specifications

Form

Liquid

Additional notes

Affinity purified.

General info

Function

Deubiquitinating enzyme that participates in a wide range of cellular processes by specifically cleaving isopeptide bonds between ubiquitin and substrate proteins or ubiquitin itself. Affects thereby important cellular signaling pathways such as NF-kappa-B, Wnt/beta-catenin, and cytokine production by regulating ubiquitin-dependent protein degradation. Participates in the activation of the Wnt signaling pathway by promoting FOXM1 deubiquitination and stabilization that induces the recruitment of beta-catenin to Wnt target gene promoter (PubMed : 26912724). Regulates the assembly and disassembly of heat-induced stress granules by mediating the hydrolysis of unanchored ubiquitin chains (PubMed : 29567855). Promotes lipopolysaccharide-induced apoptosis and inflammatory response by stabilizing the TXNIP protein (PubMed : 37534934). Affects T-cell biology by stabilizing the inhibitory receptor on T-cells PDC1 (PubMed : 37208329). Acts as a negative regulator of autophagy by regulating ULK1 at both protein and mRNA levels (PubMed : 37607937). Acts also as a negative regulator of type I interferon production by simultaneously removing both 'Lys-48'-linked unanchored and 'Lys-63'-linked anchored polyubiquitin chains on the transcription factor IRF3 (PubMed : 39761299). Modulates the stability of DNA mismatch repair protein MLH1 and counteracts the effect of the ubiquitin ligase UBR4 (PubMed : 39032648). Upon activation by insulin, it gets phosphorylated through mTORC1-mediated phosphorylation to enhance YTHDF1 stability by removing 'Lys-11'-linked polyubiquitination (PubMed : 39900921). May also deubiquitinate other substrates such as the calcium channel CACNA1H (By similarity).

Sequence similarities

Belongs to the peptidase C19 family.

Post-translational modifications

Ubiquitinated by SMURF1; leading to proteasomal degradation.. SUMOylated at Lys-113; SUMOylation affects the interaction with Cav3.2 channels.

Product protocols

Target data

Deubiquitinating enzyme that participates in a wide range of cellular processes by specifically cleaving isopeptide bonds between ubiquitin and substrate proteins or ubiquitin itself. Affects thereby important cellular signaling pathways such as NF-kappa-B, Wnt/beta-catenin, and cytokine production by regulating ubiquitin-dependent protein degradation. Participates in the activation of the Wnt signaling pathway by promoting FOXM1 deubiquitination and stabilization that induces the recruitment of beta-catenin to Wnt target gene promoter (PubMed : 26912724). Regulates the assembly and disassembly of heat-induced stress granules by mediating the hydrolysis of unanchored ubiquitin chains (PubMed : 29567855). Promotes lipopolysaccharide-induced apoptosis and inflammatory response by stabilizing the TXNIP protein (PubMed : 37534934). Affects T-cell biology by stabilizing the inhibitory receptor on T-cells PDC1 (PubMed : 37208329). Acts as a negative regulator of autophagy by regulating ULK1 at both protein and mRNA levels (PubMed : 37607937). Acts also as a negative regulator of type I interferon production by simultaneously removing both 'Lys-48'-linked unanchored and 'Lys-63'-linked anchored polyubiquitin chains on the transcription factor IRF3 (PubMed : 39761299). Modulates the stability of DNA mismatch repair protein MLH1 and counteracts the effect of the ubiquitin ligase UBR4 (PubMed : 39032648). Upon activation by insulin, it gets phosphorylated through mTORC1-mediated phosphorylation to enhance YTHDF1 stability by removing 'Lys-11'-linked polyubiquitination (PubMed : 39900921). May also deubiquitinate other substrates such as the calcium channel CACNA1H (By similarity).
See full target information USP5

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