TRIP13 Antibody (C-term) Blocking Peptides
- Known as:
- TRIP13 Antibody (C-terminus) Blocking Peptides
- Catalog number:
- BP12636b
- Product Quantity:
- 2
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- TRIP13 Antibody (C-term) Blocking Peptides
Related genes to: TRIP13 Antibody (C-term) Blocking Peptides
- Gene:
- TRIP13 NIH gene
- Name:
- thyroid hormone receptor interactor 13
- Previous symbol:
- -
- Synonyms:
- 16E1BP
- Chromosome:
- 5p15.33
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-04
- Date modifiied:
- 2016-10-05
Related products to: TRIP13 Antibody (C-term) Blocking Peptides
Related articles to: TRIP13 Antibody (C-term) Blocking Peptides
- Venetoclax-based therapies have revolutionized acute myeloid leukemia (AML) treatment, yet disease progression remains a challenge due to limited response and acquired drug resistance. Identifying molecular drivers of AML progression and resistance is essential for improving therapeutic outcomes. Genes normally silenced in normal tissues but aberrantly activated in cancers, such as Cancer-Testis (CT) genes, are promising targets for cancer diagnostics and therapy. Through a CRISPR screen focused on CT genes and cancer-associated genes exhibiting a CT-like expression profile (CT-like gene), we identified the ATPase TRIP13 as critical for AML progression while dispensable for normal hematopoiesis in genetic mouse models. Mechanistically, we discovered that TRIP13 localizes to mitochondria, where it interacts with apoptosis-inducing factor (AIF), a component of respiratory complex I. This interaction promotes leukemia progression and confers drug resistance by preventing AIF translocation to the nucleus, thereby reducing apoptotic priming and shifting energy metabolism from glycolysis to oxidative phosphorylation (OXPHOS) coupled with increased fatty acid oxidation (FAO). Genetic or pharmacological disruption of the TRIP13-AIF interaction suppressed OXPHOS, reduced leukemia cell viability, and overcame venetoclax resistance in vitro and in vivo. These findings uncover a novel mechanism by which AML cells exploit germline programs to sustain progression and resist therapy, positioning the TRIP13-AIF interaction as a promising therapeutic target for AML. - Source: PubMed
Publication date: 2026/06/13
Zhu YaoLiu HongcaiWang FuqiangLi MinjieWang NanaZhan ShuyueSun WenjieLi ShengxiWang XunWang LinZhang LianjunGu Zhimin - Significant interindividual differences exist in the efficacy of immunotherapy for hepatocellular carcinoma (HCC), and reliable biomarkers for predicting therapeutic response are lacking. Immunogenic cell death (ICD) participates in regulating the tumor immune microenvironment (TME) through the release of damage-associated molecular patterns (DAMPs), thereby possessing the potential to reshape the TME. DAMPs are essential for the occurrence of ICD. This study aims to address the lack of systematic evaluation of ICD-related molecular subtypes in HCC by constructing a DAMP-related molecular classification system and risk scoring model, as well as identifying hub genes regulating ICD in HCC for prognosis assessment and prediction of immunotherapy response. - Source: PubMed
Hu HaoYuan LehongSong ZewenTan JuanNi ZixuanLiu YangZhang Xi - Letrozole is a first-line aromatase inhibitor for estrogen receptor-positive (ER +) breast cancer, yet resistance occurs in 20-30% of patients, significantly limiting therapeutic benefit. The absence of reliable pretreatment biomarkers remains a major barrier to precision therapy. This study aimed to identify robust prognostic biomarkers and elucidate molecular mechanisms underlying letrozole resistance through integrative bioinformatics, molecular docking, and cell-based functional assays. Weighted gene co-expression network analysis of transcriptomic datasets revealed a module strongly associated with nonresponse. From this, seven candidate genes (BUB1B, CENPU, KIF11, RRM2, NUSAP1, TRIP13, PRC1) were identified as significantly overexpressed in tumors and consistently correlated with poor survival in ER + breast cancer. Among them, RRM2 emerged as the most clinically relevant marker. Molecular docking demonstrated a potential competitive interaction between RRM2 and letrozole, implicating disruption of aromatase inhibition and DNA replication pathways in resistance, while functional assays in ER + cell lines showed that RRM2 modulates proliferation and MYC-CCND1 signaling. Validation in an independent letrozole-treated cohort confirmed the strong prognostic value of RRM2. These findings provide novel mechanistic insights into endocrine resistance and establish RRM2 as a pivotal prognostic biomarker and therapeutic target. This work offers a strong foundation for biomarker-guided strategies to optimize treatment and overcome resistance in ER + breast cancer. - Source: PubMed
Publication date: 2026/05/21
Hung Wan-YuHuang Shih-ChunChen Shou-TungLin Chi-ChenHou Ming-Hon - Thyroid hormone receptor-interacting protein 13 (TRIP13), an enzyme from the AAA-ATPase family, facilitates the assembly or disassembly of protein complexes and participates in various biological processes. However, its impact on cancer immune infiltration and pan-cancer prognosis remains largely unexplored. - Source: PubMed
Publication date: 2026/04/22
Zhao YuanqiaoZhao YongqiLiu RuilinLi JingWang Yinhuai - The synaptonemal complex (SC) is a highly ordered proteinaceous structure that assembles between homologous chromosomes during the prophase I of meiosis. Conserved as a tripartite architecture across species, the SC plays a central role in chromosome synapsis, meiotic recombination, and faithful chromosome segregation. This review marks the 70th anniversary of the discovery of the synaptonemal complex by Montrose Moses in 1956. In mammals, the SC is composed of eight core (canonical) structural proteins: SYCP1, SYCP2, SYCP3, SYCE1, SYCE2, SYCE3, SIX6OS1, and TEX12. The archetypal SC consists of two lateral elements (SYCP2 and SYCP3), a central element (SYCE1/2/3, SIX6OS1, and TEX12), and numerous transverse filaments (SYCP1). A shared structural feature of SC components is the presence of coiled-coil domains. Although the tripartite organization of the SC is evolutionarily conserved, its constituent proteins exhibit little to no sequence homology across species. In addition to these core components, a number of proteins, including HORMAD1, HORMAD2, TRIP13, SKP1, CDCA5 (Sororin), UBE2I (UBC9), SYCP2L, HSPA2, PSMA8, and FKBP6, associate with the SC. Beyond serving as a structural scaffold essential for homolog synapsis, SC proteins interact with key recombination factors such as DMC1, RAD51, and TEX11, thereby regulating recombination progression and crossover formation. Genetic, biochemical, and structural analyses of SC components have provided important mechanistic insights into SC assembly and function, as well as their clinical relevance to non-obstructive azoospermia (NOA) and premature ovarian insufficiency (POI) in humans. - Source: PubMed
Publication date: 2026/04/30
Yang FangWang P Jeremy