h USP11 inducible lentiviral particles
- Known as:
- h USP11 inducible lentiviral beads
- Catalog number:
- LVP654
- Product Quantity:
- 1x107 IFU/ml x 200ul
- Category:
- -
- Supplier:
- GenTarget
- Gene target:
- USP11 inducible lentiviral particles
Related genes to: h USP11 inducible lentiviral particles
- Gene:
- USP11 NIH gene
- Name:
- ubiquitin specific peptidase 11
- Previous symbol:
- -
- Synonyms:
- UHX1
- Chromosome:
- Xp11.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-01
- Date modifiied:
- 2016-10-05
Related products to: h USP11 inducible lentiviral particles
136 kDa double-stranded RNA-binding protein,ADAR,ADAR1,Double-stranded RNA-specific adenosine deaminase,DRADA,DSRAD,G1P1,Homo sapiens,Human,IFI4,IFI-4,Interferon-inducible protein 4,K88DSRBP,p13615-oxoprostaglandin 13-reductase,D3T-inducible gene 1 protein,Dig1,DIG-1,Dithiolethione-inducible gene 1 protein,Ltb4dh,NADP-dependent leukotriene B4 12-hydroxydehydrogenase,PRG-1,Prostaglandin reduct15E1.1,Homo sapiens,HSPC132,Human,p53CSV,p53-inducible cell-survival factor,Protein 15E1.1,TP53-regulated inhibitor of apoptosis 1,TRIAP1,WF-115e1.1,Mouse,Mus musculus,p53CSV,p53-inducible cell-survival factor,Protein 15E1.1,TP53-regulated inhibitor of apoptosis 1,Triap1,WF-13-keto acyl-CoA synthase Elovl3,Cig30,CIN-2,Cold-inducible glycoprotein of 30 kDa,Elongation of very long chain fatty acids protein 3,Elovl3,Mouse,Mus musculus3-keto acyl-CoA synthase ELOVL3,CIG30,Cold-inducible glycoprotein of 30 kDa,Elongation of very long chain fatty acids protein 3,ELOVL3,Homo sapiens,Human33,ERBB receptor feedback inhibitor 1,Errfi1,Gene 33 polypeptide,Mig6,MIG-6,Mitogen-inducible gene 6 protein homolog,RALT,Rat,Rattus norvegicus,Receptor-associated late transducer6Ckine,Beta-chemokine exodus-2,C-C motif chemokine 21b,Ccl21b,Mouse,Mus musculus,Scya21,Scya21b,Small-inducible cytokine A21b,TCA4,Thymus-derived chemotactic agent 46Ckine,Beta-chemokine exodus-2,C-C motif chemokine 21c,Ccl21c,Mouse,Mus musculus,Scya21c,Small-inducible cytokine A21c,TCA4,Thymus-derived chemotactic agent 4A18 hnRNP,A18HNRNP,CIRBP,CIRP,Cold-inducible RNA-binding protein,Glycine-rich RNA-binding protein CIRP,Homo sapiens,HumanA18 hnRNP,Cirbp,Cirp,Cold-inducible RNA-binding protein,Glycine-rich RNA-binding protein CIRP,Mouse,Mus musculusA18 hnRNP,Cirbp,Cirp,Cold-inducible RNA-binding protein,Glycine-rich RNA-binding protein CIRP,Rat,Rattus norvegicusAccuCount Blank Particles, 106_mL, 13.0-17.9 μm, 10 mLAccuCount Blank Particles, 106_mL, 2.0-2.4 μm, 10 mLAccuCount Blank Particles, 106_mL, 5.0-5.9 μm, 10 mL Related articles to: h USP11 inducible lentiviral particles
- To explore the role and mechanism of X-linked USP11 in mitochondrial dysfunction associated with depression. - Source: PubMed
Feng YuqiLi NingyuanZhang LingfengWang WeiDuan HaoSun SiqiLi RuilingZhang YuhuiSong XinhuaZhang YingyueZhang HonghanNie ZhaowenYan HanchunWang ChaoLiu Zhongchun - To explore the regulatory role of SENP1 in ferroptosis of differentiated thyroid cancer cells and its molecular mechanism. - Source: PubMed
Zhu FeifeiYan NaYang JiwenChen XiaoleiWang Yingying - Rta and Zta are transcription factors expressed by Epstein-Barr virus (EBV) during the immediate-early stage of the lytic cycle. While these two proteins do not interact directly, they bind to a scaffold protein, RanBPM, to synergistically activate the transcription of EBV lytic genes. Earlier studies have shown that both Rta and Zta are destabilized through ubiquitination, which plays a crucial role in influencing EBV's lytic development. It is also known that Rta's ubiquitination is facilitated by the ubiquitin E3 ligase, RNF4. In this study, we show that RNF4 also promotes the ubiquitination of Zta. Meanwhile, a deubiquitinase, ubiquitin-specific protease (USP11), is known to interact with RanBPM. When tethered to RanBPM, Rta and Zta are deubiquitinated and stabilized by USP11. While host cells may utilize ubiquitination as a defense mechanism to destabilize Rta and Zta, thereby restricting EBV proliferation, EBV exploits RanBPM and the deubiquitination of Rta and Zta as a counter-defense strategy that favors EBV lytic replication. This study uncovers the interplay between the host and the viral mechanisms involving RNF4 and USP11 in modulating EBV lytic progression.IMPORTANCEEpstein-Barr virus (EBV) is known to express two crucial transcription factors, Rta and Zta, which are essential for activating the transcription of viral lytic genes. These two proteins are indispensable for viral lytic proliferation. While Rta and Zta can function independently to promote transcription, they also cooperate synergistically, leading to robust expression of EBV lytic proteins. In an earlier study, we showed that this synergy requires the formation of a complex involving Rta, Zta, and RanBPM at the Zta response elements in EBV lytic promoters. Recent studies showed that, despite their importance, these transcription factors are destabilized by ubiquitination, potentially serving as a mechanism through which the host restricts EBV proliferation. This study shows that EBV exploits USP11, which interacts with RanBPM, to deubiquitinate and stabilize Rta and Zta. The stabilization by USP11 is critical for EBV to overcome host-imposed restrictions and maximize its lytic proliferation. - Source: PubMed
Publication date: 2026/05/21
Chen Chi-YuanChen Po-ChunLu Yi-ShanLin Xin-RuYang Ya-ChunLee Yi-KaiCheng Zi-YunChang Shu-YinChiu Ya-FangChang Li-Kwan - The ubiquitin-specific proteases (USPs) family is the largest family of human deubiquitinating enzymes (DUBs). While most USPs are agnostic to polyubiquitin linkage-type, their substrate specificity is thought to be mediated by the recognition of the ubiquitnated protein itself. In addition to their catalytic domain, USPs have one or more auxiliary domains (ADs) with key functions in regulating DUB activity and localization. We hypothesize that some ADs bind short linear motifs (SLiMs) typically found in intrinsically disordered regions of proteins to achieve targeting to substrates and multiprotein complexes. To test this, we systematically assess the potential of 29 USP-ADs and two full-length USPs for SLiM binding using a combination of proteomic-peptide phage display, peptide SPOT arrays and affinity measurements. We discover SLiM-based interactions for 14 ADs from 9 USP-DUBs, including CYLD, USP11, USP19, USP20, USP22 and USP33, and define the consensus motif and properties of the SLiM-AD binding. Interestingly, we establish that the zf-UBP and DUSP2 domains of USP20 and USP33 are SLiM binding ADs with similar binding profiles, explaining the functional redundancy between the two DUBs. Our work reveals unique motifs recognized by the auxiliary domains CAP-Gly, UBL, zf-UBP and DUSP, with potential functional implications for substrate recognition and complex assemblies. - Source: PubMed
Publication date: 2026/05/18
Konstantinou AimilianiCórdova-Pérez AliciaVarga Julia KMadhu PriyankaSimonetti LeandroVieler MaximilianIshimura RyosukeLamoliatte FredericSchueler-Furman OraDavey Norman EKulathu YogeshIvarsson Ylva - Oxidative stress is identified as a potential factor in vitiligo pathogenesis. We aimed here to evaluate whether USP11 regulates the oxidative stress of melanocytes in vitiligo. Human melanocyte PIG1 cells were induced with 1 mM HO and pre-infected with lentiviruses for genetic intervention. The dorsal skin of C57BL/6J mice was applied with 5% HO, and genetic intervention was elicited through adenoviruses. USP11, SIRT3, and TRIM28 were reduced in melanocytes (Melan-A positive) from vitiligo mouse skin tissues and in the HO-induced PIG1 cells. TRIM28 transcriptionally activated USP11 to promote deubiquitination of SIRT3. HO decreased viability and melanin and tyrosinase contents and increased apoptosis and oxidative stress in PIG1 cells. HO induced severe depigmentation of the dorsal skin in mice, reduced melanin deposition in hair follicles, loss of melanocytes, and increased oxidative stress. Overexpression of either USP11 or TRIM28 inhibited HO-induced melanocyte damage and vitiligo, while combined knockdown of SIRT3 or USP11 reversed the effects of USP11 or TRIM28 overexpression. These findings suggest that TRIM28 exerts its effect by reducing oxidative stress in melanocytes through USP11-mediated SIRT3 deubiquitination. This observation provides a mechanistic insight that could inform future therapeutic exploration in vitiligo. Graphical abstract text. The diagram. TRIM28 inhibits oxidative stress damage in melanocytes and alleviates vitiligo by transcriptionally upregulating USP11 and promoting deubiquitination modification of SIRT3. - Source: PubMed
Nie XiaojuanLi YuanyuanYuan LingSun Mingxia