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
- FuncS
Supplier Data
Functional Studies - Recombinant human USP5 protein (DDDDK tag N-Terminus) (AB198421)
Activity assay using 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).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
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.
Target data
Product promise
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