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Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.; The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function.
Gene References into Functions
Smurf1 overexpression decreases USP25 protein turnover, and the E3 ligase enzymatic activity of Smurf1 is required for USP25 degradation. PMID: 29518389
USP25 directly interacted with tankyrases to promote their deubiquitination and stabilization and demonstrated that USP25 deficiency could promote the degradation of tankyrases and consequent stabilization of Axin to antagonize Wnt signaling PMID: 28619731
Results suggest inhibition of Usp25's catalytic activity upon the non-covalent binding of SUMO2 to the Usp25 SUMO-interacting motif, and found that SUMO2 can competitively block the interaction between the Usp25 ubiquitin-binding region and its ubiquitin substrates. PMID: 28538147
We detected SNPs at USP25 with associations of genome-wide significance for Inflammatory Bowel Disease. PMID: 27693347
REM Sleep Behavior Disorder patients with homozygous USP25 rs2823357 progressed to synucleinopathies faster than others. PMID: 25929833
Findings suggest that ubiquitin-specific protease 25 (USP25) as a VRK2 substrate that acts on TRiC deubiquitination. PMID: 25755282
These findings indicate that miR-200c exerts tumor-suppressive effects for NSCLC through the suppression of USP25 expression and suggests a new therapeutic application of miR-200c in the treatment of NSCLC. PMID: 24997798
USP25 is a novel deubiquitinating enzyme negatively regulating virus-induced interferon-beta production. PMID: 24260525
a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome. PMID: 22590560
Studies indicate that DUBs recycle ubiquitin by processing polyubiquitin chains to generate free ubiquitin, and can be regulated by ubiquitination or phosphorylation. PMID: 21480003
the second SH2 domain of SYK physically interacts with a tyrosine-rich, C-terminal region of USP25 independently of tyrosine phosphorylation PMID: 19909739
characterization of alternatively spliced products and tissue-specific isoforms PMID: 11597335
downregulation of USP25 gene in human lung cancer PMID: 18523997
Seven amino acids in the SIM of USP25 are sufficient for SUMO2/3-specific binding and conjugation PMID: 18538659
Data show that USP25m is regulated through alternative conjugation of ubiquitin (activating) or SUMO (inhibiting) to the same lysine residue (K99), which may promote the interaction with distinct intramolecular regulatory domains. PMID: 19440361
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Subcellular Location
Cytoplasm.; [Isoform USP25m]: Cytoplasm. Nucleus.
Protein Families
Peptidase C19 family
Tissue Specificity
Isoform USP25a is found in most adult and fetal tissues; expression is moderately high in testis, pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, but very low in peripheral blood, colon, small intestine, ovary, prostate, thymus and