Ask about this productRelated genes to: TPX2 Blocking Peptide
- Gene:
- TPX2 NIH gene
- Name:
- TPX2 microtubule nucleation factor
- Previous symbol:
- C20orf2, C20orf1
- Synonyms:
- p100, DIL-2
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-29
- Date modifiied:
- 2019-01-21
Related products to: TPX2 Blocking Peptide
Related articles to: TPX2 Blocking Peptide
- Pancreatic cancer is a highly aggressive malignancy with a 5-year relative survival rate of only 13%. Current treatment options have limited efficacy, and mRNA vaccines offer a new direction for its treatment. However, how to accurately identify antigen targets that possess tumor specificity, functional relevance, and immunogenicity remains the key bottleneck restricting the clinical translation of mRNA vaccines for pancreatic cancer. Recent clinical studies have advanced KRAS mutant vaccines and personalized neoantigen mRNA vaccines, yet most rely on single antigens or highly individualized designs, limiting scalability and broader clinical applicability. In this systematic review, we integrated evidence from public databases and experimental studies to identify and evaluate 16 potential pancreatic cancer mRNA vaccine antigens (ADAM9, WNT7A, TMOD3, MET, EFNB2, TPX2, AGPS, OSBPL9, KDM5A, NRAS, SCP-1, GAGE, RAB5A, ANO6, CHMP2B, and PAK2). All candidates were initially selected based on aberrant tumor expression and further prioritized using stratification strategies incorporating antigen-presenting cell infiltration, immune-related cell death pathways such as ferroptosis and pyroptosis, and functional relevance to tumor progression. ADAM9 and PAK2 showed high expression in pancreatic cancer and strong associations with tumor proliferation, invasion, and immune regulation. SCP-1 and GAGE, as cancer-testis antigens, exhibited high tumor specificity and immunogenic potential. In addition, KDM5A and ANO6 may enhance antitumor efficacy through modulation of ferroptosis or pyroptosis. Nevertheless, several candidates remain constrained by normal tissue expression or limited mechanistic evidence. This review provides a stratified framework for antigen prioritization and highlights key challenges in pancreatic cancer mRNA vaccine development, offering guidance for future multi-antigen vaccine design and translational immunotherapy. - Source: PubMed
Publication date: 2026/04/28
Xue YuzheYu JiaqiZhou HongkunChen WeiChen QiHu LingyuLuo RunzhouChen YingjingWang XiaoguangHe Xuesong - Gastroesophageal junction adenocarcinoma (GEJAC) is a highly lethal malignancy, and its molecular mechanisms are still not well understood. Reliable biomarkers for early diagnosis and immunotherapy are urgently needed. This study sought to identify hub genes linked to GEJAC by analyzing datasets from the Gene Expression Omnibus (GEO) and examining their correlation with immune cell infiltration. - Source: PubMed
Publication date: 2026/05/09
Zhu JianfuHe AiminZhang YujingHuang BingZhang JunliWang YingQin JingxiaoZhang Zhaohui - Accurate chromosome segregation requires dynamic kinetochore-microtubule attachments that, under the regulation of Aurora family kinases, biorient and align replicated chromosomes. In , Aurora A acts with the TPX2-related activator TPXL-1 to regulate these attachments and control spindle length. We show that, in addition to prominent spindle pole localization, TPXL-1-AurA has a chromatin-associated pool positioned between the sister kinetochores. Structural modeling and biochemical analysis support TPXL-1 directly recognizing the nucleosome acidic patch via an arginine anchor. Disrupting this interaction selectively removed chromatin-bound TPXL-1-AurA and caused chromosome missegregation, whereas elevation of the chromatin pool disrupted chromosome alignment. These opposing perturbations inversely affected kinetochore recruitment of the microtubule-binding Ska complex. These results support spatially distinct TPXL-1-AurA populations acting sequentially, with the spindle pole pool controlling spindle length by switching kinetochores out of a depolymerization-coupled state, and the chromatin pool controlling attachment stabilization to ensure biorientation prior to anaphase. - Source: PubMed
Publication date: 2026/05/06
Meaders Johnathan LRodriguez Alyssa AVariyar SmritiPark SungWooCirulli Alessandro EOegema KarenCorbett Kevin DDesai Arshad - Among cotton species, produces the strongest fibers. Examining cytoskeletal dynamics in single epidermal cells of ovules offers a direct approach to investigating fiber quality. Microtubules are major cytoskeletal components whose organization and dynamics are precisely regulated by microtubule-associated proteins (MAPs). However, information on the TPX2 family remains limited, and characterizing its features in is critical to clarifying the role of TPX2 family members in fiber strength formation. - Source: PubMed
Publication date: 2026/03/30
Duan YajieHan QianqianZeng RuihongCai YongshengNiu XiaoweiWen YuhongLiu Xiaoju - Human babesiosis caused by Babesia duncani is an emerging zoonotic disease that poses a growing threat to public health. Since the first reported case in 1991, knowledge of this pathogen has remained limited. Recent completion of the B. duncani genome sequence has accelerated research aimed at elucidating its molecular biology. During its intraerythrocytic life cycle, B. duncani is exposed to oxidative stress generated by redox reactions. In this study, we identified and characterized an antioxidant enzyme from B. duncani-thioredoxin peroxidase-2 (BdTPx-2), a member of the peroxiredoxin family. BdTPx-2 gene was amplified from both cDNA and gDNA of B. duncani, revealing an open reading frame of 792 bp with no introns. The native form, cellular localization, and immunogenicity of BdTPx-2 were determined using polyclonal antibodies raised against recombinant BdTPx-2 (rBdTPx-2) and sera from B. duncani-infected mice. Antioxidant activity was assessed using a mixed-function oxidation (MFO) assay. BdTPx-2 was recognized by sera from mice infected with B. duncani or B. microti, dogs infected with B. gibsoni, and water buffalo infected with B. orientalis, indicating that TPx-2 is conserved and exhibits cross-reactivity among Babesia species. A native protein of approximately 35 kDa was specifically detected in B. duncani lysates. The MFO assay demonstrated that BdTPx-2 inhibits the oxidation of plasmid DNA by a DTT/FeCl₃ mixture, preventing its conversion from the supercoiled to the nicked form. In BALB/c mice immunized with rBdTPx-2 and subsequently challenged with Babesia, parasite burden was significantly reduced, accompanied by elevated levels of the proinflammatory cytokine IFN-γ, suggesting a protective immune response induced by rBdTPx-2. This work characterizes TPx-2 as an antioxidant enzyme in B. duncani and provides insights into a key mechanism by which the parasite defends against oxidative stress during its intraerythrocytic stage. - Source: PubMed
Publication date: 2026/04/27
Guo JiayingZhao XiaohuiWang QianTian LiuZheng YaxinZhao Junlong