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The authors find that UCHL3 regulates COPS5 (show COPS5 Proteins)-dependent deneddylation of Cullin1, which is an essential component of SCF (show KITLG Proteins)(beta-TrCP (show BTRC Proteins)) complex and associated with SCF (show KITLG Proteins)(beta-TrCP (show BTRC Proteins)) activities. The authors further demonstrate that UCHL3 upregulates the levels of SCF (show KITLG Proteins)(beta-TrCP (show BTRC Proteins)) substrates including IFN-I receptor IFNAR1 (show IFNAR1 Proteins), which enhances IFN-I mediated signaling pathway and antiviral activity.
Study demonstrated positive correlations between the level and activity of UCHL3 and sperm characteristics and function suggesting that UCHL3 may play a role in male infertility.
Using a series of engineered protein substrates, which are similar in size yet differ in secondary structure, we demonstrate that thermal stability is a key factor that significantly affects UCH-L3 hydrolysis.
UCH-L3 is a novel regulator of epithelial-mesenchymal transition and cell migration in prostate cancer cells.
Data identified of UCHL3 as an essential deubiquitinase in adipogenesis.
impaired UCH-L3 function may contribute to the accumulation of full length UBB (show UBB Proteins)(+1) in various pathologie
1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethylester, an inhibitor that forms a covalent adduct with the active site cysteine of ubiquitin-specific proteases
Upregulation of UCH-L3 is associated with Uterine Cervical Neoplasms
Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations.
These results indicate that mono-Ub and Ub dimers may regulate the enzymatic functions of UCH-L1 (show UCHL1 Proteins) and UCH-L3, respectively, in vivo.
Data suggest that the activity of oocyte UCHL-1 (show UCHL1 Proteins) and -3 contributes to oocyte maturation by regulating the oocyte cortex and meiotic spindle.
subfertile Uchl1(gad-/-) mutant mice showed an intriguing pattern of switched UCH localization, with UCHL3 replacing UCHL1 (show UCHL1 Proteins) in the oocyte cortex
impaired UCH-L3 function may contribute to the accumulation of full length UBB (show UBA52 Proteins)(+1) in various pathologie
Results suggest that Uch-L3 enhances osteoblast differentiation through the stabilization of Smad1 (show SMAD1 Proteins) signaling
Polyubiquitinated proteins accumulate in skeletal muscle as well as in mouse embryonic fibroblasts derived from Uchl3-deficient mice.
Results suggest that UCH-L3 promotes adipogenesis by enhancing insulin (show INS Proteins) signaling in a hydrolase activity-dependent manner.
The role of ubiquitin C-terminal hydrolase (show UCHL1 Proteins) (UCH)-L3 in the regulation of AMP-activated protein kinase (show PRKAA2 Proteins) activity and whole-body energy metabolism are reportedl
UCH-L3 regulates the apical membrane recycling of the epithelial sodium channel
Data show that Uchl3 and mitofilin are differentially expressed in the hippocampi of inbred senescence-acclerated mice compared to normally-aging mice.
swine UCHL3, RIT1 (show RIT1 Proteins) and CCND3 (show CCND3 Proteins) genes were differentially expressed in tissues including small intestine, large intestine, liver, muscle, fat, lung, spleen and kidney
The protein encoded by this gene is a member of the deubiquitinating enzyme family. Members of this family are proteases that catalyze the removal of ubiquitin from polypeptides and are divided into five classes, depending on the mechanism of catalysis. This protein may hydrolyze the ubiquitinyl-N-epsilon amide bond of ubiquitinated proteins to regenerate ubiquitin for another catalytic cycle. Alternative splicing results in multiple transcript variants that encode different protein isoforms.
ubiquitin carboxyl-terminal hydrolase isozyme L3
, ubiquitin thioesterase L3
, ubiquitin thiolesterase
, ubiquitin carboxyl-terminal hydrolase-6
, ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase)
, ubiquitin carboxyl-terminal esterase L4