OTUB1
- Known as:
- OTUB1
- Catalog number:
- Y214173
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- OTUB1
Related genes to: OTUB1
- Gene:
- OTUB1 NIH gene
- Name:
- OTU deubiquitinase, ubiquitin aldehyde binding 1
- Previous symbol:
- -
- Synonyms:
- FLJ20113, FLJ40710
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-12
- Date modifiied:
- 2014-11-19
Related products to: OTUB1
anti-OTUB1 (1C12)anti-OTUB1 (1C12)anti-OTUB1 (1C12) type: Primary antibodies host: MouseAntibodies: OTUB1 HOST: Goat Clonality: pAbAntibody to Otubain 1 (OTUB1) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntibody to Otubain 1 (OTUB1) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntibody to Otubain 1 (OTUB1) Organism: Mus musculus (Mouse) Type: Polyclonal Source: RabbitAntibody to Otubain 1 (OTUB1) Organism: Mus musculus (Mouse) Type: Polyclonal Source: RabbitAntibody to Otubain 1 (OTUB1) Organism: Rattus norvegicus (Rat) Type: Polyclonal Source: RabbitAntibody to Otubain 1 (OTUB1) Organism: Rattus norvegicus (Rat) Type: Polyclonal Source: RabbitAntigens Ubiquitin thioesterase OTUB1 protein, Human, Recombinant, E.coliBiotin-linked Antibody to Otubain 1 (OTUB1); Reactivity: Homo sapiens (Human) Clonality: Polyclonal Source: RabbitBiotin-linked Antibody to Otubain 1 (OTUB1); Reactivity: Mus musculus (Mouse) Clonality: Polyclonal Source: RabbitBiotin-linked Antibody to Otubain 1 (OTUB1); Reactivity: Rattus norvegicus (Rat) Clonality: Polyclonal Source: RabbitDeubiquitinating enzyme OTUB1,Homo sapiens,hOTU1,HSPC263,Human,OTB1,OTU domain-containing ubiquitin aldehyde-binding protein 1,OTU1,OTUB1,Otubain-1,Ubiquitin thioesterase OTUB1,Ubiquitin-specific-proc Related articles to: OTUB1
- Hepatocellular carcinoma (HCC) treatment faces dual challenges: resistance to targeted therapy and low response rates to immunotherapy. These issues are rooted in the immunosuppressive tumor microenvironment (TME). Ferroptosis and autophagy, two critical cellular processes, play complex and paradoxical roles in HCC drug resistance and immunoregulation, and they interact closely. This review explores how the OTU deubiquitinase family, especially OTUB1, acts as a central hub coordinating the autophagy-ferroptosis balance. Additionally, other OTU family members, such as OTUD3, OTULIN, and OTUD6B, contribute to HCC progression by modulating similar pathways, highlighting the need for a broader therapeutic approach. Specifically, OTUD3 suppresses HIF-1α-driven angiogenesis, OTULIN inhibits NF-κB-mediated inflammation, and OTUD6B stabilizes pVHL to impede metastasis, collectively demonstrating their synergistic or antagonistic interactions with OTUB1 in reshaping the TME. This coordination drives HCC drug resistance and remodels the immune microenvironment. OTUB1 suppresses ferroptosis and maintains tumor cell survival by deubiquitinating and stabilizing key proteins like SLC7A11, GPX4, and p62. It also promotes immune escape by modulating PD-L1 stability and immune cell function. Consequently, therapeutic strategies targeting the OTU family-such as developing selective inhibitors for multiple members, using intelligent nanodelivery systems, and combining them with ferroptosis inducers or immune checkpoint inhibitors-show significant potential for reversing drug resistance and improving immunotherapy efficacy. Expanding these strategies to include other OTU members could enhance efficacy and reduce resistance. Addressing how the OTU family precisely modulates the intersection of autophagy and ferroptosis, and how it reshapes immune cell metabolism and function within the TME, is critical for developing novel combination therapies. This article provides a crucial theoretical foundation for developing novel combination strategies targeting metabolism-immune crosstalk. - Source: PubMed
Publication date: 2026/05/05
Zhao PengchengZhang Ping - Deubiquitinase-targeting chimera (DUBTAC) has recently emerged as a promising technology for inducing targeted protein stabilization (TPS). DUBTACs are heterobifunctional molecules that recruit deubiquitinases (DUBs) to induce deubiquitination and stabilization of target proteins. However, DUBTAC development has been hindered by the scarcity of DUB ligands. In this study, we report the discovery of novel covalent ligands of the OTUB1 DUB through structure-activity relationship (SAR) studies of the previously reported OTUB1 ligand EN523. Our lead compound (MS8572), which features a new heterocyclic core, covalently modified OTUB1 faster and more effectively, while also displaying enhanced stability and aqueous solubility compared to EN523. Furthermore, was selective for OTUB1 over several cysteine-containing proteins and did not inhibit the OTUB1 deubiquitinase activity. Lastly, by utilizing , we developed an effective CFTR DUBTAC. Overall, we developed new and improved OTUB1 covalent ligands, expanding the limited number of DUB ligands that can be harnessed for TPS. - Source: PubMed
Publication date: 2026/05/04
Song XiangyangWu QiongChen LiInuzuka HiroyukiZhong YueQi YihangLin YindanKabir MdXiong YanWei WenyiJin Jian - Restoring CD8⁺T cell infiltration and potentiating anti-tumor immune responses in the tumor microenvironment (TME) is critical for developing effective immunotherapies against triple-negative breast cancer(TNBC), while the regulatory role of N⁶-methyladenosine (m⁶A)-modified circular RNAs (circRNAs) in TNBC immune escape remains largely unelucidated. Whole-transcriptome microarray analysis combined with bioinformatics mining was conducted on TNBC tissues to screen circRNAs associated with immune evasion. RNA immunoprecipitation (RIP), RNA pulldown, and methylated RNA immunoprecipitation (MeRIP) assays were performed to verify the m⁶A modification of circFOXA1 and its interaction with gasdermin C (GSDMC). In vitro T cell-mediated tumor cytotoxicity assays and in vivo xenograft models in C57BL/6 mice were used to investigate the functional roles of the circFOXA1/GSDMC axis in TNBC anti-tumor immunity. Luciferase reporter and actinomycin D assays were further applied to clarify the regulatory mechanism of GSDMC on OTUB1 and programmed cell death-ligand 1 (PD-L1) expression. CircFOXA1 was identified as an m⁶A-modified circRNA with high stability and upregulation in TNBC, and its expression was significantly negatively correlated with CD8⁺T cell infiltration in TNBC tissues. Functionally, circFOXA1 induced immunosuppression in a CD8⁺T cell-dependent manner both in vitro and in vivo. Mechanistically, the m⁶A writer METTL14 mediated the m⁶A modification of circFOXA1, and the m⁶A reader YTHDF2 promoted circFOXA1 circularization. CircFOXA1 impaired immune cell-dependent tumor killing by upregulating GSDMC expression, which further enhanced OTUB1 mRNA stability at the post-transcriptional level. OTUB1-mediated deubiquitination subsequently stabilized PD-L1 protein, ultimately inhibiting CD8⁺T cell infiltration and driving TNBC immune escape. This study identifies a novel regulatory axis of m⁶A-modified circFOXA1/GSDMC/OTUB1/PD-L1 in mediating TNBC immune escape, where GSDMC enhances PD-L1 protein stability via OTUB1-dependent deubiquitination. These findings reveal a new molecular mechanism underlying TNBC immune evasion and identify circFOXA1 as a potential therapeutic target to improve the efficacy of anti-PD-1/PD-L1 immunotherapy in TNBC. - Source: PubMed
Publication date: 2026/04/22
Shen HonghongLi BoyuWen XiaoqianZhao ChangqingWang Chen - The replication protein A (RPA) complex safeguards single-stranded DNA (ssDNA) and coordinates repair during replication stress and homologous recombination (HR), but the mechanisms regulating its timely engagement and release at damage sites are not well defined. Here, we identified RNF185 as a critical E3 ligase that orchestrates temporally distinct patterns of RPA1 ubiquitination-shifting from K6/K63- to K48-linked chains-to precisely regulate HR and replication fork restart upon DNA damage. Mechanistically, RNF185 undergoes ATM/ATR-dependent phosphorylation at threonine 106 and translocates into the nucleus via interaction with NUP88 following DSBs. In the early response phase, RNF185 promotes K6/K63-linked ubiquitination of RPA1, stabilizing RPA1 on ssDNA to facilitate replication fork restart and efficient recruitment of RPA1 to damage sites. At later stages, RNF185 competes with the deubiquitinase OTUB1 for RPA1 binding and facilitates K48-linked ubiquitination at lysine 458, promoting RPA1 degradation and its removal from chromatin. Loss of RNF185 disrupts RPA1 turnover, impairs HR efficiency, destabilizes replication forks, and sensitizes tumor cells to irradiation and cisplatin. In vivo, RNF185 depletion significantly enhances the therapeutic efficacy of radiotherapy. In summary, this study demonstrates that RNF185 is a key regulatory factor in HR and replication fork restart, aiding cells in their response to radio- or chemotherapy induced DNA damage in clinical settings. - Source: PubMed
Publication date: 2026/04/15
Yao ZhichengWang RuruChen BinZhao XipengZhang JieZhou ShenglanXu AnWu LijunZhang JieXu FengZhao Guoping - Osseointegration in patients with type 2 diabetes mellitus (T2DM) is poor, and overcoming osseointegration impairment safely and efficiently remains challenging. - Source: PubMed
Publication date: 2026/04/13
Wang LingxiaoDiao ZhanqiuWang WanqingHuang YishuLiu YangGao ZhenhuaMa PanShan ZhaochenLi JunFan Zhipeng