Recombinant Human USP25 protein (Tagged)
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Recombinant Human USP25 protein (Tagged) is a Human Fragment protein, in the 162 to 677 aa range, expressed in Escherichia coli, with >75%, suitable for SDS-PAGE.
View Alternative Names
USP21, USP25, Ubiquitin carboxyl-terminal hydrolase 25, Deubiquitinating enzyme 25, USP on chromosome 21, Ubiquitin thioesterase 25, Ubiquitin-specific-processing protease 25
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human USP25 protein (Tagged) (AB269120)
SDS-PAGE analysis of ab269120.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
USP25 contributes to the modulation of several key proteins by rescuing them from proteasomal degradation through deubiquitination. This protein is involved in multiple cellular processes such as signal transduction and the immune response. USP25 is part of the endoplasmic reticulum-associated degradation (ERAD) complex where it functions to recycle ubiquitin molecules from substrates destined for degradation. By doing so USP25 influences the stability and localization of various proteins impacting cell growth and survival.
Pathways
USP25 is involved in the ubiquitin-proteasome system (UPS) and the Wnt signaling pathway. In the UPS USP25 interacts with proteins like LRP6 helping regulate the amount of ß-catenin thereby influencing Wnt signaling activity. This interaction plays a role in controlling cell proliferation and differentiation. USP25 also associates with other deubiquitinating enzymes reflecting its role in multiple regulatory pathways essential for cellular function.
Specifications
Form
Liquid
General info
Function
Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions in various biological processes including inflammation, immune response (PubMed : 29518389, PubMed : 37683630). Modulates the Wnt/beta-catenin pathway by deubiquitinating and stabilizing tankyrases TNKS1 and TNKS2 (PubMed : 28619731, PubMed : 30926243). Regulates KEAP1-NRF2 axis in the defense against oxidative assaults by deubiquitinating KEAP1 and protecting it from degradation leading to degradation of the NRF2 transcription factor that is responsible for mounting an anti-oxidation gene expression program (PubMed : 37339955). Positively regulates RNA virus-induced innate signaling by interacting with and deubiquitinating ERLIN1 and ERLIN2 (PubMed : 37683630). In turn, restricts virus production by regulating cholesterol biosynthetic flux (PubMed : 37683630). Acts as a negative regulator of interleukin-17-mediated signaling and inflammation through the removal of 'Lys-63'-linked ubiquitination of TRAF5 and TRAF6 (PubMed : 23042150). Prevents the ubiquitination and degradation of TRAF3 to reduce the phosphorylation levels of JNK and P38, the secretion of IL-1B and to induce endotoxin tolerance (PubMed : 30579117).. The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function.
Sequence similarities
Belongs to the peptidase C19 family.
Post-translational modifications
Acetylated.. Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP1. Polyubiquitinated by SMURF1 by promoting the 'Lys-48'-linkage leading to proteasomal degradation (PubMed:29518389).. Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions.. Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels.
Subcellular localisation
Nucleus
Target data
Product promise
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